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31 results on '"Faida H."'

1. 1H-Imidazole-2,5-Dicarboxamides as NS4A Peptidomimetics: Identification of a New Approach to Inhibit HCV-NS3 Protease

Author

Abdelsattar M. Omar, Mahmoud A. Elfaky, Stefan T. Arold, Sameh H. Soror, Maan T. Khayat, Hani Z. Asfour, Faida H. Bamane, and Moustafa E. El-Araby

Subjects
ns3 inhibitors, allosteric inhibitors, ns4a, peptidomimetics, imidazole, hepatitis c virus, molecular dynamics, flaviviridae, dsls, binding assay, Microbiology, QR1-502
Abstract

The nonstructural (NS) protein NS3/4A protease is a critical factor for hepatitis C virus (HCV) maturation that requires activation by NS4A. Synthetic peptide mutants of NS4A were found to inhibit NS3 function. The bridging from peptide inhibitors to heterocyclic peptidomimetics of NS4A has not been considered in the literature and, therefore, we decided to explore this strategy for developing a new class of NS3 inhibitors. In this report, a structure-based design approach was used to convert the bound form of NS4A into 1H-imidazole-2,5-dicarboxamide derivatives as first generation peptidomimetics. This scaffold mimics the buried amino acid sequence Ile-25` to Arg-28` at the core of NS4A21`−33` needed to activate the NS3 protease. Some of the synthesized compounds (Coded MOC) were able to compete with and displace NS4A21`−33` for binding to NS3. For instance, N5-(4-guanidinobutyl)-N2-(n-hexyl)-1H-imidazole-2,5-dicarboxamide (MOC-24) inhibited the binding of NS4A21`−33` with a competition half maximal inhibitory concentration (IC50) of 1.9 ± 0.12 µM in a fluorescence anisotropy assay and stabilized the denaturation of NS3 by increasing the aggregation temperature (40% compared to NS4A21`−33`). MOC-24 also inhibited NS3 protease activity in a fluorometric assay. Molecular dynamics simulations were conducted to rationalize the differences in structure−activity relationship (SAR) between the active MOC-24 and the inactive MOC-26. Our data show that MOC compounds are possibly the first examples of NS4A peptidomimetics that have demonstrated promising activities against NS3 proteins.

Published
2020
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2. Theonellamide G, a Potent Antifungal and Cytotoxic Bicyclic Glycopeptide from the Red Sea Marine Sponge Theonella swinhoei

Author

Diaa T. A. Youssef, Lamiaa A. Shaala, Gamal A. Mohamed, Jihan M. Badr, Faida H. Bamanie, and Sabrin R. M. Ibrahim

Subjects
Theonella swinhoei, glycopeptide, theonellamide G, antifungal activity, cytotoxic activity, Biology (General), QH301-705.5
Abstract

In our search for bioactive metabolites from marine organisms, we have investigated the polar fraction of the organic extract of the Red Sea sponge Theonella swinhoei. Successive chromatographic separations and final HPLC purification of the potent antifungal fraction afforded a new bicyclic glycopeptide, theonellamide G (1). The structure of the peptide was determined using extensive 1D and 2D NMR and high-resolution mass spectral determinations. The absolute configuration of theonellamide G was determined by chemical degradation and 2D NMR spectroscopy. Theonellamide G showed potent antifungal activity towards wild and amphotericin B-resistant strains of Candida albicans with IC50 of 4.49 and 2.0 μM, respectively. Additionally, it displayed cytotoxic activity against the human colon adenocarcinoma cell line (HCT-16) with IC50 of 6.0 μM. These findings provide further insight into the chemical diversity and biological activities of this class of compounds.

Published
2014
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3. Aryloxyalkanoic Acids as Non-Covalent Modifiers of the Allosteric Properties of Hemoglobin

Author

Abdelsattar M. Omar, Mona A. Mahran, Mohini S. Ghatge, Faida H. A. Bamane, Mostafa H. Ahmed, Moustafa E. El-Araby, Osheiza Abdulmalik, and Martin K. Safo

Subjects
hemoglobin, sickle cell disease, aryloxyalkanoic acids, halogenated benzene, imidazole, antisickling, oxygen equilibrium curve, high affinity, low affinity, crystal structure, Organic chemistry, QD241-441
Abstract

Hemoglobin (Hb) modifiers that stereospecifically inhibit sickle hemoglobin polymer formation and/or allosterically increase Hb affinity for oxygen have been shown to prevent the primary pathophysiology of sickle cell disease (SCD), specifically, Hb polymerization and red blood cell sickling. Several such compounds are currently being clinically studied for the treatment of SCD. Based on the previously reported non-covalent Hb binding characteristics of substituted aryloxyalkanoic acids that exhibited antisickling properties, we designed, synthesized and evaluated 18 new compounds (KAUS II series) for enhanced antisickling activities. Surprisingly, select test compounds showed no antisickling effects or promoted erythrocyte sickling. Additionally, the compounds showed no significant effect on Hb oxygen affinity (or in some cases, even decreased the affinity for oxygen). The X-ray structure of deoxygenated Hb in complex with a prototype compound, KAUS-23, revealed that the effector bound in the central water cavity of the protein, providing atomic level explanations for the observed functional and biological activities. Although the structural modification did not lead to the anticipated biological effects, the findings provide important direction for designing candidate antisickling agents, as well as a framework for novel Hb allosteric effectors that conversely, decrease the protein affinity for oxygen for potential therapeutic use for hypoxic- and/or ischemic-related diseases.

Published
2016
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5. Correction: Epidemiology and outcomes of early-onset AKI in COVID-19-related ARDS in comparison with non-COVID-19-related ARDS: insights from two prospective global cohort studies (Critical Care, (2023), 27, 1, (3), 10.1186/s13054-022-04294-5)

Author

McNicholas B. A., Mcnicholas, B, Rezoagli, E, Simpkin, A, Khanna, S, Suen, J, Yeung, P, Brodie, D, Bassi, G, Pham, T, Bellani, G, Fraser, J, Laffey, J, Al-Dabbous, T, Alfoudri, H, Shamsah, M, Alhadad, Q, Hanan, M, Elapavaluru, S, Berg, A, Horn, C, Abdelhalim, A, Amer, A, Elnaggar, C, Hassan, A, Abdelaziz, A, Abdelhalim, M, Orabi, Y, Alaraji, Z, Muhaisen, M, Almasri, L, Mustafa, D, Hamdan, S, Al-Saba'a, Y, Dalloul, Z, Alkahlout, M, Jaber, H, Aldabbourosama, O, Hussein, A, Emad, Z, Khaled, S, Mohamed, N, Hassanin, E, Hamdi, A, Ragab, A, Azizeldin, M, Mayasi, Y, Schroll, S, Meyer, D, Velazco, J, Ploskanych, L, Fikes, W, Bagewadi, R, Dao, M, White, H, Laviena, A, Ehlers, A, Shalabi-McGuire, M, Witt, T, Grazioli, L, Lorini, L, Grandin, E, Nunez, J, Reyes, T, O'Briain, D, Hunter, S, Ramanan, M, Affleck, J, Veerendra, H, Rai, S, Russell-Brown, J, Nourse, M, Joseph, M, Mitchell, B, Tenzer, M, Abe, R, Cho, H, Jeong, I, Rahman, N, Kakar, V, Sun, H, Hanley, A, Brozzi, N, Mehkri, O, Krishnan, S, Duggal, A, Houltham, S, Graf, J, Diaz, R, Orrego, R, Delgado, C, Gonzalez, J, Sanchez, M, Piagnerelli, M, Sarrazin, J, Zabert, G, Espinosa, L, Delgado, P, Delgado, V, Rincon, D, Yanten, A, Duque, M, Abouelmagd, K, Elhazmi, A, Al-Hudaib, A, Javidfar, J, Callahan, M, Dong, A, D'Orleans, C, Taufik, M, Wardoyo, E, Gunawan, M, Trisnaningrum, N, Irawany, V, Rayhan, M, Panigada, M, Pesenti, A, Zanella, A, Grasselli, G, Colombo, S, Martinet, C, Florio, G, Antonelli, M, Carelli, S, Grieco, D, Asaki, M, Hoshino, K, Salazar, L, Monsalve, M, Cosgrave, D, Atif, M, Qutishat, F, Laffey, C, Van Der Walt, M, Mccaffrey, J, Bone, A, Hakeem, Y, Winearls, J, Tallott, M, Thomson, D, Joubert, I, Arnold-Day, C, Piercy, J, van Zyl Smit, R, Miller, M, Seymour, L, van Heyningen, F, Teyangesikayi, G, Fredericks, D, Hssain, A, Aliudin, J, Alqahtani, A, Mohamed, K, Mohamed, A, Tan, D, Villanueva, J, Zaqout, A, Kurtzman, E, Ademi, A, Dobrita, A, El Aoudi, K, Segura, J, Giwangkancana, G, Ohshimo, S, Osatnik, J, Joosten, A, Torres, A, Yang, M, Motos, A, Luna, C, Arancibia, F, Williams, V, Noel, A, Luque, N, Fantini, M, Garcia, R, Alvarez, E, Greti, A, Ceccato, A, Sanchez, A, Vazquez, A, Roche-Campo, F, Franch-Llasat, D, Tuazon, D, Amato, M, Cassimiro, L, Pola, F, Ribeiro, F, Fonseca, G, Dalton, H, Desai, M, Osborn, E, Deeb, H, Arcadipane, A, Martucci, G, Panarello, G, Vitiello, S, Bianco, C, Occhipinti, G, Rossetti, M, Cuffaro, R, Cho, S, Whitman, G, El Sayed, M, Mokhtar, W, El-Shenawy, E, Shimizu, H, Moriyama, N, Kim, J, Kitamura, N, Gebauer, J, Yokoyama, T, Al-Fares, A, Buabbas, S, Alamad, E, Alawadhi, F, Alawadi, K, Khalefa, M, Al Ajeel, N, Aly, M, Al-Saleh, A, Naanouh, A, Elshourbgy, A, Gad, M, Elrazaz, R, Khadadah, I, Almumin, A, Altarakma, H, Albannay, H, Alsaleh, M, Radwan, M, Saadallah, I, Tanaka, H, Hashimoto, S, Yamazaki, M, Oh, T, Epler, M, Forney, C, Kruse, L, Feister, J, Williamson, J, Grobengieser, K, Gnall, E, Golden, S, Caroline, M, Shapiro, T, Karaj, C, Thome, L, Sher, L, Vanderland, M, Welch, M, Mcdermott, S, Brain, M, Mineall, S, Unwin, M, Chen, L, Trezise, T, Mckeon, L, Kimura, D, Brazzi, L, Sales, G, Montrucchio, G, Ogston, T, Nagpal, D, Fischer, K, Lorusso, R, van Bussell, B, De Piero, M, Mariani, S, Rangappa, R, Shetty, R, Rai, P, Ganesan, A, Esperatti, M, Fuentes, N, Gonzalez, M, Carton, E, Sen, A, Palacios, A, Rainey, D, Samoukoviv, G, Campisi, J, Durham, L, Neumann, E, Seefeldt, C, Falcucci, O, Emmrich, A, Guy, J, Johns, C, Potzner, K, Zimmermann, C, Espinal, A, Buchtele, N, Schwameis, M, Korhnfehl, A, Brock, R, Staudinger, T, Stecher, S, Barnikel, M, Anton, S, Pawlikowski, A, Zaaqoq, A, Galloway, L, Merley, C, Nichol, A, Csete, M, Quesada, L, Saba, I, Kasugai, D, Hiraiwa, H, Tanaka, T, Marwali, E, Purnama, Y, Dewayanti, S, Ardiyan, Juzar, D, Siagian, D, Chen, Y, Ogino, M, Nasa, P, Matthew, C, Majeed, N, Ratsep, I, Post, A, Sillaots, P, Krund, A, Lehiste, M, Lepik, T, Manetta, F, Mihelis, E, Sarmiento, I, Narasimhan, M, Varrone, M, Komats, M, Garcia-Diaz, J, Harmon, C, Satyapriya, S, Bhatt, A, Mokadam, N, Uribe, A, Gonzalez, A, Shi, H, Mckeown, J, Pasek, J, Fiorda, J, Echeverria, M, Moreno, R, Zakhary, B, Cavana, M, Cucino, A, Foti, G, Giani, M, Fumagalli, B, Chiumello, D, Castagna, V, Dell'Amore, A, Navalesi, P, Shum, H, Vuysteke, A, Usman, A, Acker, A, Smood, B, Mergler, B, Sertic, F, Subramanian, M, Sperry, A, Rizer, N, Burhan, E, Rasmin, M, Akmal, E, Sitompul, F, Lolong, N, Naivedh, B, Erickson, S, Barrett, P, Dean, D, Daugherty, J, Loforte, A, Khan, I, Quraishi, M, Desantis, O, So, D, Kandamby, D, Mandei, J, Natanael, H, Yudhalantang, E, Lantang, A, Wijaya, S, Jung, A, Ng, G, Ng, W, Ng, P, Fang, S, Tabah, A, Ratcliffe, M, Duroux, M, Alajeeli, A, Tarhabat, A, Adachi, S, Nakao, S, Blanco, P, Prieto, A, Sanchez, J, Nicholson, M, Butt, W, Serratore, A, Delzoppo, C, Janin, P, Yarad, E, Totaro, R, Coles, J, Pujo, B, Balk, R, Vissing, A, Kapania, E, Hays, J, Fox, S, Yantosh, G, Mishin, P, Yuliarto, S, Santoso, K, Djajalaksana, S, Fatoni, A, Fukuda, M, Liu, K, Pelosi, P, Battaglini, D, Jimenez, J, Bastos, D, Gaiao, S, Rusmawatiningtyas, D, Cho, Y, Lee, S, Kawasaki, T, Munshi, L, Sakiyalak, P, Nitayavardhana, P, Elagili, M, Salem, T, Seitz, T, Arora, R, Kent, D, Marino, D, Parwar, S, Cheng, A, Miller, J, Fujitani, S, Shimizu, N, Madhok, J, Owyang, C, Buscher, H, Reynolds, C, Maasikas, O, Aleksanbeljantsev, Mihnovits, V, Akimoto, T, Aizawa, M, Horibe, K, Onodera, R, Hodgson, C, Burrell, A, Young, M, George, T, Shekar, K, Mcguinness, N, Irvine, L, Flynn, B, Endo, T, Sugiyama, K, Shimizu, K, Fan, E, Exconde, K, Ichiba, S, Binnawara, M, Lussier, L, Lotz, G, Malfertheiner, M, Maier, L, Dreier, E, Kusumastuti, N, Mccloskey, C, Dabaliz, A, Elshazly, T, Smith, J, Szuldrzynski, K, Bielanski, P, Wille, K, Murthy, S, Parhar, K, Fiest, K, Codan, C, Shahid, A, Fayed, M, Evans, T, Gutierrez, A, Song, T, Rose, R, Bennett, S, Richardson, D, Peek, G, Arora, L, Rappapport, K, Rudolph, K, Sibenaller, Z, Stout, L, Walter, A, Herr, D, Vedadi, N, Bartlett, R, Thompson, S, Hoffman, J, Ying, X, Williams, B, Sanchez, E, Akwani, C, Kennedy, R, Elhadi, M, Griffee, M, Mone, M, Ciullo, A, Kida, Y, Roca, R, Riera, J, Contreras, S, Alegre, C, Kay, C, Fischer, I, Renner, E, Taniguci, H, Lee, J, Plotkin, D, Citarella, B, Merson, L, Hartley, E, Lubis, B, Ikeyama, T, Alhamad, A, Fathi, M, Hadhoud, M, Alhouri, H, Mechi, A, Alyasiri, M, Elsaid, M, Shahla, H, Bhaskar, B, Jung, J, Mcguinness, S, Eastwood, G, Marta, S, Guarracino, F, Gerle, S, Coxon, E, Claro, B, Eleisawy, M, Osama, H, Loverde, D, Patil, N, Parrini, V, Mcbride, A, Negaard, K, Ratsch, A, Uribe, J, Peris, A, Sanders, M, Emerson, D, Kamal, M, Faida, H, Povoa, P, Francis, R, Cherif, A, Joseph, S, Di Nardo, M, Heard, M, Kyle, K, Blackwell, R, Ouyahia, A, Biston, P, Jeong, H, Smith, R, Prawira, Y, Garcia, A, Salterain, N, Meyns, B, Elnasser, M, Moreno, M, Walia, R, Mehta, A, Schweda, A, Williams, M, Emadamkhatirah, Kim, K, Assad, A, Giraldo, E, Karolak, W, Balik, M, Pocock, E, Gajkowski, E, Masafumi, K, Barrett, N, Takeyama, Y, Park, S, Amin, F, Andriyani, F, Sudakevych, S, Schnur, J, Vera, M, Cornejo, R, Schwarz, P, Mardini, A, de Paula, T, Neto, A, Villoldo, A, Colafranceschi, A, Iglesias, A, Granjean, J, Melro, L, Romualdo, G, Gaia, D, Souza, H, Galas, F, Mendiluce, R, Sosa, A, Martinez, I, Kurosawa, H, Almoshantaf, M, Salgado, J, Hugi-Mayr, B, Charbonneau, E, Barzilai, V, Monteiro, V, de Souza, R, Harper, M, Siddig, N, Suzuki, H, Adams, C, Brieva, J, Khamees, A, Graige, F, Supriatna, M, Nyale, G, Eltatar, F, Fatani, J, Baeissa, H, Masri, A, Rabie, A, Hui, M, Yamane, M, Jung, H, Margaret, A, Nacpil, N, Ruck, K, Bakken, R, Jara, C, Felton, T, Tharwat, S, Berra, L, Shah, B, Chakraborty, A, Cardona, M, Capatos, G, Akkanti, B, Orija, A, Jain, H, Ito, A, Muftah, M, Housni, B, Aldhalia, A, Low, S, Iihara, K, Chavez, J, Ramanathan, K, Naidoo, K, Seppelt, I, Vandyk, M, Macdonald, S, Hafez, W, Mcgregor, R, Siebenaler, T, Flynn, H, Lofton, K, Aokage, T, Kvirkvelia, B, Shigemitsu, K, Moscatelli, A, Fiorentino, G, Baumgaertel, M, Mba, S, Assy, J, Hutahaean, A, Roush, H, Sichting, K, Alessandri, F, Burns, D, Alkhubouli, T, Nasrallah, A, Salt, G, Garabedian, C, Millar, J, Sim, M, Mattke, A, Mcauley, D, Tadili, J, Frenzel, T, Bar-Lavie, Y, Ortiz, A, Stone, J, Attokaran, A, Farquharson, M, Patel, B, Gunning, D, Baillie, K, Adem, S, Watson, P, Tamai, K, Sajinadiyasa, G, Kanyawati, D, Salgado, M, Sassine, A, Yudo, B, Mccaul, S, Lee, B, Afek, A, Iwashita, Y, Fadlalmola, H, Semedi, B, Mansour, N, Metiva, J, Van Belle, N, Martin-Loeches, I, Al-Sadawi, M, Kirakli, C, Shimaa, A, Abdurraouf, A, Ivatt, L, Moharam, S, Woon, C, Kang, H, Smith, T, James, E, Al-Rawas, N, Almjersah, A, Iwasaki, Y, Ashour, H, Embarek, H, King-Chung, K, Gudzenko, V, Taccone, F, Perdhana, F, Lamarche, Y, Ribeiro, J, Bradic, N, Van den Bossche, K, Lansink, O, Singh, G, Debeuckelaere, G, Stelfox, H, Yi, C, Elia, J, Tribble, T, Shankar, S, Padmanabhan, R, Hallinan, B, Paoletti, L, Leyva, Y, Fykuda, T, Badulak, J, Koch, J, Janowaik, L, Hackman, A, Hernandez, D, Osofsky, J, Donadello, K, Lawang, A, Fine, J, Davidson, B, Abdehaleem, I, McNicholas B. A., Rezoagli E., Simpkin A. J., Khanna S., Suen J. Y., Yeung P., Brodie D., Bassi G. L., Pham T., Bellani G., Fraser J. F., Laffey J., Al-Dabbous T., Alfoudri H., Shamsah M., Alhadad Q., Hanan M., Elapavaluru S., Berg A., Horn C., Abdelhalim A. R. M. E., Amer A. E., Elnaggar C. O. R., Hassan A. A., Abdelaziz A., Abdelhalim M., Orabi Y. S. S. A., Alaraji Z. A., Muhaisen M. R., Almasri L., Mustafa D., Hamdan S., Al-Saba'a Y., Dalloul Z., Alkahlout M., Jaber H., Aldabbourosama O., Hussein A. A. R. M., Emad Z. K., Khaled S., Mohamed N., Hassanin E., Hamdi A., Ragab A., Azizeldin M. G., Mayasi Y., Schroll S., Meyer D., Velazco J., Ploskanych L., Fikes W., Bagewadi R., Dao M., White H., Laviena A. B., Ehlers A., Shalabi-McGuire M., Witt T., Grazioli L., Lorini L., Grandin E. W., Nunez J., Reyes T., O'Briain D., Hunter S., Ramanan M., Affleck J., Veerendra H. H., Rai S., Russell-Brown J., Nourse M., Joseph M., Mitchell B., Tenzer M., Abe R., Cho H. J., Jeong I. S., Rahman N., Kakar V., Sun H., Hanley A., Brozzi N., Mehkri O., Krishnan S., Duggal A., Houltham S., Graf J., Diaz R., Orrego R., Delgado C., Gonzalez J., Sanchez M. S., Piagnerelli M., Sarrazin J. V., Zabert G., Espinosa L., Delgado P., Delgado V., Rincon D. F. B., Yanten A. M. M., Duque M. B., Abouelmagd K., Elhazmi A., Al-Hudaib A., Javidfar J., Callahan M., Dong A., D'Orleans C. C., Taufik M. A., Wardoyo E. Y., Gunawan M., Trisnaningrum N. S., Irawany V., Rayhan M., Panigada M., Pesenti A., Zanella A., Grasselli G., Colombo S., Martinet C., Florio G., Antonelli M., Carelli S., Grieco D. L., Asaki M., Hoshino K., Salazar L., Monsalve M. A. M., McNicholas B., Cosgrave D., Atif M., Qutishat F., Laffey C., Van Der Walt M., McCaffrey J., Bone A., Hakeem Y., Winearls J., Tallott M., Thomson D., Joubert I., Arnold-Day C., Piercy J., van Zyl Smit R., Miller M., Seymour L., van Heyningen F., Teyangesikayi G., Fredericks D., Hssain A. A., Aliudin J., Alqahtani A. -R., Mohamed K., Mohamed A., Tan D., Villanueva J., Zaqout A., Kurtzman E., Ademi A., Dobrita A., El Aoudi K., Segura J., Giwangkancana G., Ohshimo S., Osatnik J., Joosten A., Torres A., Yang M., Motos A., Luna C., Arancibia F., Williams V., Noel A., Luque N., Fantini M., Garcia R. N. J., Alvarez E. C., Greti A., Ceccato A., Sanchez A., Vazquez A. L., Roche-Campo F., Franch-Llasat D., Tuazon D., Amato M., Cassimiro L., Pola F., Ribeiro F., Fonseca G., Dalton H., Desai M., Osborn E., Deeb H., Arcadipane A., Martucci G., Panarello G., Vitiello S., Bianco C., Occhipinti G., Rossetti M., Cuffaro R., Cho S. -M., Whitman G., El Sayed M., Mokhtar W., El-Shenawy E., Shimizu H., Moriyama N., Kim J. -B., Kitamura N., Gebauer J., Yokoyama T., Al-Fares A., Buabbas S., Alamad E., Alawadhi F., Alawadi K., Khalefa M. A., Al Ajeel N. A. A., Aly M. F., Al-Saleh A., Naanouh A., Elshourbgy A. M., Gad M. Y., ElRazaz R. M., Khadadah I., Almumin A. M., Altarakma H., Albannay H., Alsaleh M. K., Radwan M. S. A., Saadallah I. A., Tanaka H., Hashimoto S., Yamazaki M., Oh T. -H., Epler M., Forney C., Kruse L., Feister J., Williamson J., Grobengieser K., Gnall E., Golden S., Caroline M., Shapiro T., Karaj C., Thome L., Sher L., Vanderland M., Welch M., McDermott S., Brain M., Mineall S., Unwin M., Chen L., Trezise T., McKeon L., Kimura D., Brazzi L., Sales G., Montrucchio G., Ogston T., Nagpal D., Fischer K., Lorusso R., van Bussell B., De Piero M. E., Mariani S., Rangappa R., Shetty R. M., Rai P. S., Ganesan A., Esperatti M., Fuentes N. A., Gonzalez M. E., Carton E. G., Sen A., Palacios A., Rainey D., Samoukoviv G., Campisi J., Durham L., Neumann E., Seefeldt C., Falcucci O., Emmrich A., Guy J., Johns C., Potzner K., Zimmermann C., Espinal A., Buchtele N., Schwameis M., Korhnfehl A., Brock R., Staudinger T., Stecher S. -S., Barnikel M., Anton S., Pawlikowski A., Zaaqoq A., Galloway L. A., Merley C., Nichol A., Csete M., Quesada L., Saba I., Kasugai D., Hiraiwa H., Tanaka T., Marwali E., Purnama Y., Dewayanti S. R., Juzar D. A., Siagian D., Chen Y. -S., Ogino M., Nasa P., Matthew C., Majeed N. A., Ratsep I., Post A. -M., Sillaots P., Krund A., Lehiste M. -H., Lepik T., Manetta F., Mihelis E., Sarmiento I. C., Narasimhan M., Varrone M., Komats M., Garcia-Diaz J., Harmon C., Satyapriya S. V., Bhatt A., Mokadam N. A., Uribe A., Gonzalez A., Shi H., McKeown J., Pasek J., Fiorda J., Echeverria M., Moreno R., Zakhary B., Cavana M., Cucino A., Foti G., Giani M., Fumagalli B., Chiumello D., Castagna V., Dell'Amore A., Navalesi P., Shum H. -P., Vuysteke A., Usman A., Acker A., Smood B., Mergler B., Sertic F., Subramanian M., Sperry A., Rizer N., Burhan E., Rasmin M., Akmal E., Sitompul F., Lolong N., Naivedh B., Erickson S., Barrett P., Dean D., Daugherty J., Loforte A., Khan I., Quraishi M. A., DeSantis O., So D., Kandamby D., Mandei J. M., Natanael H., YudhaLantang E., Lantang A., Wijaya S. O., Jung A., Ng G., Ng W. Y., Ng P. Y., Fang S., Tabah A., Ratcliffe M., Duroux M., Alajeeli A., Tarhabat A., Adachi S., Nakao S., Blanco P., Prieto A., Sanchez J., Nicholson M., Butt W., Serratore A., Delzoppo C., Janin P., Yarad E., Totaro R., Coles J., Pujo B., Balk R., Vissing A., Kapania E., Hays J., Fox S., Yantosh G., Mishin P., Yuliarto S., Santoso K. H., Djajalaksana S., Fatoni A. Z., Fukuda M., Liu K., Pelosi P., Battaglini D., Jimenez J. F. M., Bastos D., Gaiao S., Rusmawatiningtyas D., Cho Y. -J., Lee S. H., Kawasaki T., Munshi L., Sakiyalak P., Nitayavardhana P., Elagili M. B., Salem T. A. A., Seitz T., Arora R., Kent D., Marino D., Parwar S., Cheng A., Miller J., Fujitani S., Shimizu N., Madhok J., Owyang C., Buscher H., Reynolds C., Maasikas O., AleksanBeljantsev, Mihnovits V., Akimoto T., Aizawa M., Horibe K., Onodera R., Hodgson C., Burrell A., Young M., George T., Shekar K., McGuinness N., Irvine L., Flynn B., Endo T., Sugiyama K., Shimizu K., Fan E., Exconde K., Ichiba S., Binnawara M., Lussier L., Lotz G., Malfertheiner M., Maier L., Dreier E., Kusumastuti N. P., McCloskey C., Dabaliz A. -A., Elshazly T. B., Smith J., Szuldrzynski K. S., Bielanski P., Wille K., Murthy S., Parhar K. K. S., Fiest K. M., Codan C., Shahid A., Fayed M., Evans T., Garcia R., Gutierrez A., Song T., Rose R., Bennett S., Richardson D., Peek G., Arora L., Rappapport K., Rudolph K., Sibenaller Z., Stout L., Walter A., Herr D., Vedadi N., Bartlett R., Thompson S., Hoffman J., Ying X., Williams B., Sanchez E., Akwani C., Kennedy R., Elhadi M., Griffee M., Mone M., Ciullo A., Kida Y., Roca R. F., Riera J. I., Contreras S., Alegre C., Kay C., Fischer I., Renner E., Taniguci H., Lee J., Plotkin D., Citarella B. W., Merson L., Hartley E., Lubis B., Ikeyama T., Alhamad A., Fathi M., Hadhoud M. M., Alhouri H., Mechi A., Alyasiri M. S., Elsaid M. Z. A., Shahla H., Bhaskar B., Jung J. -S., McGuinness S., Eastwood G., Marta S. R., Guarracino F., Gerle S., Coxon E., Claro B., Eleisawy M., Osama H., Loverde D., Patil N., Parrini V., McBride A., Negaard K., Ratsch A., Uribe J. D., Peris A., Sanders M., Emerson D., Kamal M., Faida H., Povoa P., Francis R., Cherif A., Joseph S., Di Nardo M., Heard M., Kyle K., Blackwell R. A., Ouyahia A., Biston P., Jeong H. W., Smith R., Prawira Y., Garcia A. H., Salterain N., Meyns B., Elnasser M., Moreno M., Walia R., Mehta A., Schweda A., Williams M., EmadAmkhatirah, Kim K. H., Assad A., Giraldo E., Karolak W., Balik M., Pocock E., Gajkowski E., Masafumi K., Barrett N., Takeyama Y., Park S., Amin F., Andriyani F. M., Sudakevych S., Schnur J., Vera M., Cornejo R., Schwarz P., Mardini A. C., de Paula T., Neto A. S., Villoldo A., Colafranceschi A. S., Iglesias A. U., Granjean J., Melro L. M. G., Romualdo G. F., Gaia D., Souza H., Galas F., Mendiluce R. M., Sosa A., Martinez I., Kurosawa H., Almoshantaf M. B., Salgado J., Hugi-Mayr B., Charbonneau E., Barzilai V. S., Monteiro V., de Souza R. R., Harper M., Siddig N., Suzuki H., Adams C., Brieva J., Khamees A., Graige F., Supriatna M., Nyale G., Eltatar F. S., Fatani J., Baeissa H., Masri A. A. L., Rabie A., Hui M. Y., Yamane M., Jung H., Margaret A. M., Nacpil N., Ruck K., Bakken R., Jara C., Felton T., Tharwat S., Berra L., Shah B., Chakraborty A., Cardona M., Capatos G., Akkanti B., Orija A., Jain H., Ito A., Muftah M., Housni B., Aldhalia A., Low S., Iihara K., Chavez J., Ramanathan K., Naidoo K., Seppelt I., VanDyk M., MacDonald S., Hafez W., McGregor R., Siebenaler T., Flynn H., Lofton K., Aokage T., Kvirkvelia B., Shigemitsu K., Moscatelli A., Fiorentino G., Baumgaertel M., Mba S. E., Assy J., Hutahaean A., Roush H., Sichting K. A., Alessandri F., Burns D., Alkhubouli T. H., Nasrallah A., Salt G., Garabedian C. P., Millar J., Sim M., Mattke A., McAuley D., Tadili J., Frenzel T., Bar-Lavie Y., Ortiz A. B., Stone J., Attokaran A., Farquharson M., Patel B., Gunning D., Baillie K., Adem S., Watson P., Tamai K., Sajinadiyasa G. K., Kanyawati D., Salgado M., Sassine A., Yudo B., McCaul S., Lee B., Lee S. M., Afek A., Iwashita Y., Fadlalmola H., Semedi B. P., Mansour N. M., Metiva J., Van Belle N., Martin-Loeches I., Al-Sadawi M., Kirakli C., Shimaa A. -T., Abdurraouf A., Ivatt L., Moharam S., Woon C. Y., Kang H. M., Smith T., James E., Al-Rawas N., Almjersah A., Iwasaki Y., Ashour H., Embarek H., King-Chung K. C., Gudzenko V., Taccone F., Perdhana F., Lamarche Y., Ribeiro J. M., Bradic N., Van den Bossche K., Lansink O., Singh G., Debeuckelaere G., Stelfox H. T., Yi C., Elia J., Tribble T., Shankar S., Padmanabhan R., Hallinan B., Paoletti L., Leyva Y., Fykuda T., Badulak J., Koch J., Janowaik L., Hackman A., Hernandez D., Osofsky J., Donadello K., Lawang A., Fine J., Davidson B., Vazquez A. O. R., Abdehaleem I., McNicholas B. 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A., Aliudin J., Alqahtani A. -R., Mohamed K., Mohamed A., Tan D., Villanueva J., Zaqout A., Kurtzman E., Ademi A., Dobrita A., El Aoudi K., Segura J., Giwangkancana G., Ohshimo S., Osatnik J., Joosten A., Torres A., Yang M., Motos A., Luna C., Arancibia F., Williams V., Noel A., Luque N., Fantini M., Garcia R. N. J., Alvarez E. C., Greti A., Ceccato A., Sanchez A., Vazquez A. L., Roche-Campo F., Franch-Llasat D., Tuazon D., Amato M., Cassimiro L., Pola F., Ribeiro F., Fonseca G., Dalton H., Desai M., Osborn E., Deeb H., Arcadipane A., Martucci G., Panarello G., Vitiello S., Bianco C., Occhipinti G., Rossetti M., Cuffaro R., Cho S. -M., Whitman G., El Sayed M., Mokhtar W., El-Shenawy E., Shimizu H., Moriyama N., Kim J. -B., Kitamura N., Gebauer J., Yokoyama T., Al-Fares A., Buabbas S., Alamad E., Alawadhi F., Alawadi K., Khalefa M. A., Al Ajeel N. A. A., Aly M. F., Al-Saleh A., Naanouh A., Elshourbgy A. M., Gad M. Y., ElRazaz R. M., Khadadah I., Almumin A. M., Altarakma H., Albannay H., Alsaleh M. K., Radwan M. S. A., Saadallah I. A., Tanaka H., Hashimoto S., Yamazaki M., Oh T. -H., Epler M., Forney C., Kruse L., Feister J., Williamson J., Grobengieser K., Gnall E., Golden S., Caroline M., Shapiro T., Karaj C., Thome L., Sher L., Vanderland M., Welch M., McDermott S., Brain M., Mineall S., Unwin M., Chen L., Trezise T., McKeon L., Kimura D., Brazzi L., Sales G., Montrucchio G., Ogston T., Nagpal D., Fischer K., Lorusso R., van Bussell B., De Piero M. E., Mariani S., Rangappa R., Shetty R. M., Rai P. S., Ganesan A., Esperatti M., Fuentes N. A., Gonzalez M. E., Carton E. G., Sen A., Palacios A., Rainey D., Samoukoviv G., Campisi J., Durham L., Neumann E., Seefeldt C., Falcucci O., Emmrich A., Guy J., Johns C., Potzner K., Zimmermann C., Espinal A., Buchtele N., Schwameis M., Korhnfehl A., Brock R., Staudinger T., Stecher S. -S., Barnikel M., Anton S., Pawlikowski A., Zaaqoq A., Galloway L. A., Merley C., Nichol A., Csete M., Quesada L., Saba I., Kasugai D., Hiraiwa H., Tanaka T., Marwali E., Purnama Y., Dewayanti S. R., Juzar D. A., Siagian D., Chen Y. -S., Ogino M., Nasa P., Matthew C., Majeed N. A., Ratsep I., Post A. -M., Sillaots P., Krund A., Lehiste M. -H., Lepik T., Manetta F., Mihelis E., Sarmiento I. C., Narasimhan M., Varrone M., Komats M., Garcia-Diaz J., Harmon C., Satyapriya S. V., Bhatt A., Mokadam N. A., Uribe A., Gonzalez A., Shi H., McKeown J., Pasek J., Fiorda J., Echeverria M., Moreno R., Zakhary B., Cavana M., Cucino A., Foti G., Giani M., Fumagalli B., Chiumello D., Castagna V., Dell'Amore A., Navalesi P., Shum H. -P., Vuysteke A., Usman A., Acker A., Smood B., Mergler B., Sertic F., Subramanian M., Sperry A., Rizer N., Burhan E., Rasmin M., Akmal E., Sitompul F., Lolong N., Naivedh B., Erickson S., Barrett P., Dean D., Daugherty J., Loforte A., Khan I., Quraishi M. A., DeSantis O., So D., Kandamby D., Mandei J. M., Natanael H., YudhaLantang E., Lantang A., Wijaya S. O., Jung A., Ng G., Ng W. Y., Ng P. Y., Fang S., Tabah A., Ratcliffe M., Duroux M., Alajeeli A., Tarhabat A., Adachi S., Nakao S., Blanco P., Prieto A., Sanchez J., Nicholson M., Butt W., Serratore A., Delzoppo C., Janin P., Yarad E., Totaro R., Coles J., Pujo B., Balk R., Vissing A., Kapania E., Hays J., Fox S., Yantosh G., Mishin P., Yuliarto S., Santoso K. H., Djajalaksana S., Fatoni A. Z., Fukuda M., Liu K., Pelosi P., Battaglini D., Jimenez J. F. M., Bastos D., Gaiao S., Rusmawatiningtyas D., Cho Y. -J., Lee S. H., Kawasaki T., Munshi L., Sakiyalak P., Nitayavardhana P., Elagili M. B., Salem T. A. A., Seitz T., Arora R., Kent D., Marino D., Parwar S., Cheng A., Miller J., Fujitani S., Shimizu N., Madhok J., Owyang C., Buscher H., Reynolds C., Maasikas O., AleksanBeljantsev, Mihnovits V., Akimoto T., Aizawa M., Horibe K., Onodera R., Hodgson C., Burrell A., Young M., George T., Shekar K., McGuinness N., Irvine L., Flynn B., Endo T., Sugiyama K., Shimizu K., Fan E., Exconde K., Ichiba S., Binnawara M., Lussier L., Lotz G., Malfertheiner M., Maier L., Dreier E., Kusumastuti N. P., McCloskey C., Dabaliz A. -A., Elshazly T. B., Smith J., Szuldrzynski K. S., Bielanski P., Wille K., Murthy S., Parhar K. K. S., Fiest K. M., Codan C., Shahid A., Fayed M., Evans T., Garcia R., Gutierrez A., Song T., Rose R., Bennett S., Richardson D., Peek G., Arora L., Rappapport K., Rudolph K., Sibenaller Z., Stout L., Walter A., Herr D., Vedadi N., Bartlett R., Thompson S., Hoffman J., Ying X., Williams B., Sanchez E., Akwani C., Kennedy R., Elhadi M., Griffee M., Mone M., Ciullo A., Kida Y., Roca R. F., Riera J. I., Contreras S., Alegre C., Kay C., Fischer I., Renner E., Taniguci H., Lee J., Plotkin D., Citarella B. W., Merson L., Hartley E., Lubis B., Ikeyama T., Alhamad A., Fathi M., Hadhoud M. M., Alhouri H., Mechi A., Alyasiri M. S., Elsaid M. Z. A., Shahla H., Bhaskar B., Jung J. -S., McGuinness S., Eastwood G., Marta S. R., Guarracino F., Gerle S., Coxon E., Claro B., Eleisawy M., Osama H., Loverde D., Patil N., Parrini V., McBride A., Negaard K., Ratsch A., Uribe J. D., Peris A., Sanders M., Emerson D., Kamal M., Faida H., Povoa P., Francis R., Cherif A., Joseph S., Di Nardo M., Heard M., Kyle K., Blackwell R. A., Ouyahia A., Biston P., Jeong H. W., Smith R., Prawira Y., Garcia A. H., Salterain N., Meyns B., Elnasser M., Moreno M., Walia R., Mehta A., Schweda A., Williams M., EmadAmkhatirah, Kim K. H., Assad A., Giraldo E., Karolak W., Balik M., Pocock E., Gajkowski E., Masafumi K., Barrett N., Takeyama Y., Park S., Amin F., Andriyani F. M., Sudakevych S., Schnur J., Vera M., Cornejo R., Schwarz P., Mardini A. C., de Paula T., Neto A. S., Villoldo A., Colafranceschi A. S., Iglesias A. U., Granjean J., Melro L. M. G., Romualdo G. F., Gaia D., Souza H., Galas F., Mendiluce R. M., Sosa A., Martinez I., Kurosawa H., Almoshantaf M. B., Salgado J., Hugi-Mayr B., Charbonneau E., Barzilai V. S., Monteiro V., de Souza R. R., Harper M., Siddig N., Suzuki H., Adams C., Brieva J., Khamees A., Graige F., Supriatna M., Nyale G., Eltatar F. S., Fatani J., Baeissa H., Masri A. A. L., Rabie A., Hui M. Y., Yamane M., Jung H., Margaret A. M., Nacpil N., Ruck K., Bakken R., Jara C., Felton T., Tharwat S., Berra L., Shah B., Chakraborty A., Cardona M., Capatos G., Akkanti B., Orija A., Jain H., Ito A., Muftah M., Housni B., Aldhalia A., Low S., Iihara K., Chavez J., Ramanathan K., Naidoo K., Seppelt I., VanDyk M., MacDonald S., Hafez W., McGregor R., Siebenaler T., Flynn H., Lofton K., Aokage T., Kvirkvelia B., Shigemitsu K., Moscatelli A., Fiorentino G., Baumgaertel M., Mba S. E., Assy J., Hutahaean A., Roush H., Sichting K. A., Alessandri F., Burns D., Alkhubouli T. H., Nasrallah A., Salt G., Garabedian C. P., Millar J., Sim M., Mattke A., McAuley D., Tadili J., Frenzel T., Bar-Lavie Y., Ortiz A. B., Stone J., Attokaran A., Farquharson M., Patel B., Gunning D., Baillie K., Adem S., Watson P., Tamai K., Sajinadiyasa G. K., Kanyawati D., Salgado M., Sassine A., Yudo B., McCaul S., Lee B., Lee S. M., Afek A., Iwashita Y., Fadlalmola H., Semedi B. P., Mansour N. M., Metiva J., Van Belle N., Martin-Loeches I., Al-Sadawi M., Kirakli C., Shimaa A. -T., Abdurraouf A., Ivatt L., Moharam S., Woon C. Y., Kang H. M., Smith T., James E., Al-Rawas N., Almjersah A., Iwasaki Y., Ashour H., Embarek H., King-Chung K. C., Gudzenko V., Taccone F., Perdhana F., Lamarche Y., Ribeiro J. M., Bradic N., Van den Bossche K., Lansink O., Singh G., Debeuckelaere G., Stelfox H. T., Yi C., Elia J., Tribble T., Shankar S., Padmanabhan R., Hallinan B., Paoletti L., Leyva Y., Fykuda T., Badulak J., Koch J., Janowaik L., Hackman A., Hernandez D., Osofsky J., Donadello K., Lawang A., Fine J., Davidson B., Vazquez A. O. R., and Abdehaleem I.

Abstract

Following publication of the original article [1], the authors identified that the collaborating authors part of the collaborating author group CCCC Consortium was missing. The collaborating author group is available and included as Additional file 1 in this article.

Published
2023

6. Design, Synthesis, Molecular Modeling and Anti-Hyperglycemic Evaluation of Quinazoline-Sulfonylurea Hybrids as Peroxisome Proliferator-Activated Receptor Gamma (PPARγ) and Sulfonylurea Receptor (SUR) Agonists

Author

Mohamed Ayman El-Zahabi, Faida H. Bamanie, Salah Ghareeb, Heba K. Alshaeri, Moudi M. Alasmari, Mohamed Moustafa, Zohair Al-Marzooki, and Mohamed F. Zayed

Subjects
Organic Chemistry, General Medicine, Sulfonylurea Receptors, Catalysis, Computer Science Applications, Diabetes Mellitus, Experimental, Rats, Inorganic Chemistry, Molecular Docking Simulation, PPAR gamma, design, synthesis, quinazoline, sulfonylurea, anti-hyperglycemic, Sulfonylurea Compounds, Glyburide, Quinazolines, Animals, Humans, Hypoglycemic Agents, Physical and Theoretical Chemistry, Molecular Biology, Spectroscopy
Abstract

New quinazoline-sulfonylurea hybrids were prepared and examined for their in vivo anti-hyperglycemic activities in STZ-induced hyperglycemic rats using glibenclamide as a reference drug. Compounds VI-6-a, V, IV-4, VI-4-c, IV-6, VI-2-a, IV-1, and IV-2 were more potent than the reference glibenclamide. They induced significant reduction in the blood glucose levels of diabetic rats: 78.2, 73.9, 71.4, 67.3, 62, 60.7, 58.4, and 55.9%, respectively, while the reference glibenclamide had 55.4%. Compounds IV-1, VI-2-a, IV-2, V, and IV-6 showed more prolonged antidiabetic activity than glibenclamide. Moreover, molecular docking and pharmacokinetic studies were performed to examine binding modes of the prepared compounds against peroxisome proliferator-activated receptor gamma (PPARγ). The highest active compounds exhibited good binding affinity with high free energy of binding against PPARγ. In silico absorption, distribution, metabolism, elimination and toxicity (ADMET) studies were performed to investigate pharmacokinetics and safety of the synthesized compounds. They showed considerable human intestinal absorption with low toxicity profile.

Published
2022
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7. Design, Synthesis, Molecular Modeling and Anti-Hyperglycemic Evaluation of Quinazoline-Sulfonylurea Hybrids as Peroxisome Proliferator-Activated Receptor Gamma (PPARγ) and Sulfonylurea Receptor (SUR) Agonists

Author

El-Zahabi, Mohamed Ayman, primary, Bamanie, Faida H., additional, Ghareeb, Salah, additional, Alshaeri, Heba K., additional, Alasmari, Moudi M., additional, Moustafa, Mohamed, additional, Al-Marzooki, Zohair, additional, and Zayed, Mohamed F., additional

Published
2022
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8. Synthetic bulky NS4A peptide variants bind to and inhibit HCV NS3 protease

Author

Maan T. Khayat, Sameh H. Soror, Faida H. Bamane, Hani Z. Asfour, Moustafa E. El-Araby, Abdelsattar M. Omar, Stefan T. Arold, and Mahmoud A. Elfaky

Subjects
0301 basic medicine, Allosteric inhibitor, viruses, medicine.medical_treatment, Allosteric regulation, Mutant, Peptide, Article, 03 medical and health sciences, 0302 clinical medicine, Peptide mutants, Catalytic triad, medicine, lcsh:Science (General), ComputingMethodologies_COMPUTERGRAPHICS, chemistry.chemical_classification, lcsh:R5-920, NS3, Multidisciplinary, Protease, Chemistry, Drug discovery, virus diseases, DSLS, NS3/4A, digestive system diseases, Amino acid, 030104 developmental biology, Biochemistry, 030220 oncology & carcinogenesis, HCV, lcsh:Medicine (General), Fluorescence anisotropy, lcsh:Q1-390
Abstract

Graphical abstract, NS4A is a non-structural multi-tasking small peptide that is essential for HCV maturation and replication. The central odd-numbered hydrophobic residues of NS4A (Val-23‘ to Leu-31‘)i are essential for activating NS3 upon NS3/4A protease complex formation. This study aims to design new specific allosteric NS3/4A protease inhibitors by mutating Val-23‘, Ile-25‘, and Ile-29‘ into bulkier amino acids. Pep-15, a synthetic peptide, showed higher binding affinity towards HCV-NS3 subtype-4 than native NS4A. The Kd of Pep-15 (80.0 ± 8.0 nM) was twice as high as that of native NS4A (169 ± 37 nM). The mutant Pep-15 inhibited the catalytic activity of HCV-NS3 by forming an inactive complex. Molecular dynamics simulations suggested that a cascade of conformational changes occurred, especially in the catalytic triad arrangements, thereby inactivating NS3. A large shift in the position of Ser-139 was observed, leading to loss of critical hydrogen bonding with His-57. Even though this study is not a classic drug discovery study—nor do we propose Pep-15 as a drug candidate—it serves as a stepping stone towards developing a potent inhibitor of hitherto untargeted HCV subtypes.

Published
2020
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14. New purine alkaloids from the Red Sea marine tunicate Symplegma rubra

Author

Faida H. Bamanie, Jihan M. Badr, Diaa T. A. Youssef, Gamal A. Mohamed, Sabrin R.M. Ibrahim, and Lamiaa A. Shaala

Subjects
Purine, biology, Kinase, Stereochemistry, Plant Science, biology.organism_classification, Biochemistry, Tunicate, chemistry.chemical_compound, chemistry, Symplegma rubra, Natural source, medicine, Inosine, Spectral data, Agronomy and Crop Science, Heteronuclear single quantum coherence spectroscopy, Biotechnology, medicine.drug
Abstract

Investigation of the Red Sea marine tunicate Symplegma rubra Monniot, 1972 gave three new purine alkaloids namely 6-methoxy-7,9-dimethyl-8-oxoguanine ( 1 ), 6-methoxy-9-methyl-8-oxoguanine ( 2 ), and 2-methoxy-7-methyl-8-oxoadenine ( 4 ) together with seven known compounds: 6-methoxy-7-methyl-8-oxoguanine ( 3 ), 9-methyl-8-oxoadenine ( 5 ), 7-methyl-8-oxoadenine ( 6 ), 8-oxoadenine ( 7 ), 3-methylxanthine ( 8 ), inosine ( 9 ), and homarine (pyridinium-2-carboxylic acid-1-methyl) ( 10 ). Compound 6 was reported here for the first time from a natural source. The structure determination of the compounds was accomplished by extensive interpretation of their spectroscopic data including 1D ( 1 H and 13 C) and 2D ( 1 H– 1 H COSY, HSQC, and HMBC) NMR and high-resolution mass spectral data. The isolated compounds were evaluated for their protein kinase inhibitory activity against different kinases (CDK5, CK1, DyrK1A, and GSK3) at 10 μg/mL. The compounds showed moderate activity against these kinases.

Published
2015
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15. Ehrenasterol and biemnic acid; new bioactive compounds from the Red Sea sponge Biemna ehrenbergi

Author

Jihan M. Badr, Gamal A. Mohamed, Diaa T. A. Youssef, Faida H. Bamanie, and Lamiaa A. Shaala

Subjects
biology, Stereochemistry, Plant Science, medicine.disease_cause, biology.organism_classification, Antimicrobial, Mass spectrometry, Biochemistry, Sterol, Sponge, chemistry.chemical_compound, chemistry, medicine, Candida albicans, Thymidine, Agronomy and Crop Science, Escherichia coli, Two-dimensional nuclear magnetic resonance spectroscopy, Biotechnology
Abstract

In continuation of our efforts to identify bioactive compounds from the Red Sea marine sponges, we have recently investigated the organic extract of the sponge Biemna ehrenbergi . This study resulted in the isolation of eight compounds including a new sterol, ehrenasterol ( 1 ), a new C 24 -acetylenic acid, biemnic acid ( 2 ), together with six known compounds including a hopanoid, three steroids and two nucleosides. The isolated compounds were identified as (22 E )-ergosta-22-ene-8,14-epoxy-3,7-dione ( 1 ), ( E )-tetracos-8-en-5-ynoic acid ( 2 ), (22 E )-ergosta-5,8,22-trien-7-one-3 β -ol ( 3 ), 32,35-anhydrobacteriohopanetetrol ( 4 ), (24 R )-ergosta-6,22-diene-5,8-epidioxy-3-ol ( 5 ), melithasterol B ( 6 ), thymidine ( 7 ) and 2′-deoxyuridine ( 8 ). The structures of the isolated compounds were assigned by different spectral data including 1D and 2D NMR (COSY, HSQC, and HMBC) and high-resolution mass spectrometry. Compound 1 displayed inhibition zone of 20 mm at 100 μg/disc against Escherichia coli in the disc diffusion assay. Similarly, compounds 2 and 4 displayed inhibition zones of 20 and 18 mm respectively against Candida albicans at the same concentration. Compounds 1 – 3 displayed weak cytotoxic activity against human colon adenocarcinoma (HCT-116) cancer cell line.

Published
2015
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16. Identification of a novel class of covalent modifiers of hemoglobin as potential antisickling agents

Author

Moustafa E. El-Araby, Nadia Chowdhury, Osheiza Abdulmalik, Abdelsattar M. Omar, Mona A. Mahran, Faida H. Bamane, Martin K. Safo, and Mohini S. Ghatge

Subjects
Models, Molecular, Cell Survival, Stereochemistry, Hemoglobin, Sickle, Allosteric regulation, Anemia, Sickle Cell, Biochemistry, Article, Cell Line, Mice, Structure-Activity Relationship, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Antisickling Agents, Animals, Humans, Structure–activity relationship, Reactivity (chemistry), Physical and Theoretical Chemistry, 030304 developmental biology, 0303 health sciences, Dose-Response Relationship, Drug, Molecular Structure, Chemistry, Organic Chemistry, Imidazoles, Oxygen transport, Glutathione, 3. Good health, Acrylates, Covalent bond, 030220 oncology & carcinogenesis, Hemoglobin, Pharmacophore
Abstract

Aromatic aldehydes and ethacrynic acid (ECA) exhibit antipolymerization properties that are beneficial for sickle cell disease therapy. Based on ECA pharmacophore and its atomic interaction with hemoglobin, we designed and synthesized several compounds--designated as KAUS (imidazolylacryloyl derivatives)--that we hypothesized would bind covalently to βCys93 of hemoglobin and inhibit sickling. The compounds surprisingly showed weak allosteric and antisickling properties. X-ray studies of hemoglobin in complex with representative KAUS compounds revealed an unanticipated mode of Michael addition reaction between the β-unsaturated carbon and the N-terminal αVal1 nitrogen at the α-cleft of hemoglobin, with no observable interaction with βCys93. Interestingly, the compounds exhibited almost no reactivity with the free amino acids, L-Val, L-His and L-Lys, however showed some reactivity with both glutathione and L-Cys. Our findings provide a molecular level explanation to the compounds biological activities and an important framework for targeted modifications that would yield novel potent antisickling agents.

Published
2015
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17. Platelet aggregation and serum adenosine deaminase (ADA) activity in pregnancy associated with diabetes, hypertension and HIV

Author

Claudio A M, Leal, Daniela B R, Leal, Stephen A, Adefegha, Vera M, Morsch, José E P, da Silva, João F P, Rezer, Clarissa M L, Schrekker, Faida H, Abdalla, and Maria R C, Schetinger

Subjects
Adult, Platelet Aggregation, Adenosine Deaminase, Platelet-Rich Plasma, HIV Infections, Adenosine Diphosphate, Diabetes, Gestational, Pregnancy, Case-Control Studies, Hypertension, Humans, Female, Blood Coagulation, Enzyme Assays
Abstract

Platelet aggregation and adenosine deaminase (ADA) activity were evaluated in pregnant women living with some disease conditions including hypertension, diabetes mellitus and human immunodeficiency virus infection. The subject population is consisted of 15 non-pregnant healthy women [control group (CG)], 15 women with normal pregnancy (NP), 7 women with hypertensive pregnancy (HP), 10 women with gestational diabetes mellitus (GDM) and 12 women with human immunodeficiency virus-infected pregnancy (HIP) groups. The aggregation of platelets was checked using an optical aggregometer, and serum ADA activity was determined using the colorimetric method. After the addition of 5 µM of agonist adenosine diphosphate, the percentage of platelet aggregation was significantly (p 0·05) increased in NP, HP, GDM and HIP groups when compared with the CG, while the addition of 10 µM of the same agonist caused significant (p 0·05) elevations in HP, GDM and HIP groups when compared with CG. Furthermore, ADA activity was significantly (p 0·05) enhanced in NP, HP, GDM and HIP groups when compared with CG. In this study, the increased platelet aggregation and ADA activity in pregnancy and pregnancy-associated diseases suggest that platelet aggregation and ADA activity could serve as peripheral markers for the development of effective therapy in the maintenance of homeostasis and some inflammatory process in these pathophysiological conditions. Copyright © 2016 John WileySons, Ltd.

Published
2016

18. APPLICATION OF HIGH PERFORMANCE THIN LAYER CHROMATOGRAPHY FOR DETERMINATION OF NICOTINE IN DIFFERENT BRANDS OF CIGARETTES

Author

Jihan M. Badr, Faida H. Bamane, and Nagwa S. El-Shaer

Subjects
Detection limit, Chromatography, biology, Nicotiana tabacum, Alkaloid, Clinical Biochemistry, Pharmaceutical Science, Absorption (skin), biology.organism_classification, Biochemistry, Thin-layer chromatography, Analytical Chemistry, Nicotine, Hexane, chemistry.chemical_compound, chemistry, medicine, High performance thin layer chromatography, medicine.drug
Abstract

There are several known methods for quantitative determination of nicotine, the main alkaloid of Nicotiana tabacum, with each presenting a series of advantages and disadvantages. As an alternative, we suggest a densitometric determination for nicotine allowing its estimation in a number of brands of cigarettes. Separation was performed by thin layer chromatography using hexane: CH2Cl2:MeOH (2:8:1.5) as a developing mixture. Densitometric measurements were carried out at the absorption maximum 254 nm. The method demonstrated good precision and accuracy, which were indicated by the low values of RSD %. Limits of detection and quantitation were recorded as 0.008 mg mL−1 and 0.02 mg mL−1, respectively. A considerable variation of nicotine content was noticed among the nine investigated brands of cigarettes where samples 3 and 8 revealed the highest amounts of nicotine that were approximately duplicated compared to other samples.

Published
2012
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19. Antioxidant activities and flavonoid contents of selected plants belonging to Family Loranthaceae

Author

Jihan M. Badr, Faida H. Bamane, and Omayma Abdel Razek M. Amin

Subjects
chemistry.chemical_classification, Antioxidant, Chromatography, biology, Chemistry, DPPH, medicine.medical_treatment, Loranthaceae, antioxidant, spectrophotometry, high performance thin layer chromatography (HPTLC), flavonoids, quercetin, ascorbic acid, Flavonoid, Loranthaceae, Ascorbic acid, biology.organism_classification, Applied Microbiology and Biotechnology, chemistry.chemical_compound, Griess test, Genetics, medicine, heterocyclic compounds, High performance thin layer chromatography, Quercetin, Agronomy and Crop Science, Molecular Biology, Biotechnology
Abstract

The methanolic extract of three parasitic plants belonging to family Loranthaceae ( Plicosepalus acacia , Plicosepalus curviflorus and Phragmanthera austro arabica ) were investigated for their antioxidant activity. The free radical and nitrogen oxide scavenging abilities were evaluated using diphenyl-1-picrylhydrazyl (DPPH), and Griess reagent was used to determine the total antioxidant activity. The three extracts showed comparable activities. The three activities ranged from 18 to 56% of the activity of standard ascorbic. The total flavonoid contents were determined and calculated in terms of quercetin which was detected in all the examined extracts. The quercetin concentration was determined using high performance thin layer chromatography using CHCl 3 : MeOH : glacial acetic acid (8.5: 1.5: 0.1) for development. The maximum sensitivity was obtained when the plates were scanned at 360 nm. The concentration of quercetin varied from 0.157 ( P. austro arabica ) to 0.062 g% ( P. acacia ) and P. curviflorus contained 0.115 g% w/w quercetin. All validation parameters were found to be satisfactory regarding accuracy, precision, limits of detection and quantitation. Key words: Loranthaceae, antioxidant, spectrophotometry, high performance thin layer chromatography (HPTLC), flavonoids, quercetin, ascorbic acid.

Published
2016

21. Analysis of abiraterone stress degradation behavior using liquid chromatography coupled to ultraviolet detection and electrospray ionization mass spectrometry

Author

Ibrahim A. Darwish, Faida H. Bamane, and Alaa Khedr

Subjects
Spectrometry, Mass, Electrospray Ionization, Trace Amounts, Ultraviolet Rays, Electrospray ionization, Clinical Biochemistry, Analytical chemistry, Pharmaceutical Science, medicine.disease_cause, Analytical Chemistry, Hydrolysis, Drug Stability, Drug Discovery, otorhinolaryngologic diseases, medicine, Photodegradation, Spectroscopy, Response factor, Detection limit, Androstenols, Chromatography, Chemistry, Reproducibility of Results, Degradation (geology), Androstenes, Spectrophotometry, Ultraviolet, Ultraviolet, Chromatography, Liquid
Abstract

A validated stability-indicating LC–UV–ESI-MS analytical method was established to analyze abiraterone (ABR) and its potential degradation products (DPs) and was performed according to ICH guidelines. Trace amounts of DPs that might be released under different environmental conditions were determined. Stress conditions, including the effect of heat, acid-base hydrolysis, oxidation and UV-light were investigated. ABR was found to be sensitive to UV light and oxidation. Five potential mono-oxygenated ABR products were generated upon exposure to UV-irradiation. Di-, tri-, and tetra-oxygenated ABR were detected and progressively increased in quantity upon longer exposure to UV light. The ESI-MS response factors (RF) of potential DPs and ABR were not comparable. The ESI-MS response factor of each single potential degradation product was derived from the LC–UV analysis of concentrated solutions of pure and degraded ABR. The ESI-MS limit of detection (LOD) and limit of quantification (LOQ) of ABR were 30 and 80 pg/μL, respectively. The intra-day RSD was 0.20%, and the inter-day RSD was 0.30%.

Published
2012

22. Brominated arginine-derived alkaloids from the red sea sponge Suberea mollis

Author

Faida H. Bamane, Diaa T. A. Youssef, Jihan M. Badr, and Lamiaa A. Shaala

Subjects
Antioxidant, Stereochemistry, DPPH, medicine.medical_treatment, Pharmaceutical Science, Antineoplastic Agents, Biology, Pharmacognosy, Arginine, Antioxidants, Analytical Chemistry, chemistry.chemical_compound, Alkaloids, Picrates, Drug Discovery, medicine, Animals, Humans, Indian Ocean, Nuclear Magnetic Resonance, Biomolecular, Pharmacology, Molecular Structure, Alkaloid, Organic Chemistry, Biphenyl Compounds, Absolute configuration, Biological activity, Antimicrobial, Hydrocarbons, Brominated, Porifera, Complementary and alternative medicine, chemistry, Molecular Medicine, Acid hydrolysis, Drug Screening Assays, Antitumor, HeLa Cells
Abstract

Investigation of a new collection of the Red Sea sponge Suberea mollis afforded two new brominated arginine-derived alkaloids, subereamines A (1) and B (2), a new brominated phenolic compound, subereaphenol D (3), and the known compounds dichloroverongiaquinol (4), aerothionin (5), and purealdin L (6). The structures of the isolated compounds were assigned using one- and two-dimensional NMR spectra and HRFABMS data. The absolute configurations of subereamines A (1) and B (2) were determined by acid hydrolysis followed by chiral-phase LC-MS. The antimicrobial and antioxidant activities of the isolated compounds have been evaluated. Dichloroverongiaquinol and subereaphenol D displayed significant antimicrobial activity. Using the DPPH TLC autographic rapid screen for free radical scavenging effects, subereaphenol D displayed a significant antioxidant effect. In addition, the cytotoxic activities of the isolated compounds were investigated.

Published
2011

25. Aryloxyalkanoic Acids as Non-Covalent Modifiers of the Allosteric Properties of Hemoglobin.

Author

Omar, Abdelsattar M., Mahran, Mona A., Ghatge, Mohini S., Bamane, Faida H. A., Ahmed, Mostafa H., El-Araby, Moustafa E., Abdulmalik, Osheiza, and Safo, Martin K.

Subjects
ALKANOIC acids, HEMOGLOBIN synthesis, ALLOSTERIC regulation, SICKLE cell anemia, ANTISICKLING agents, PREVENTION
Abstract

Hemoglobin (Hb) modifiers that stereospecifically inhibit sickle hemoglobin polymer formation and/or allosterically increase Hb affinity for oxygen have been shown to prevent the primary pathophysiology of sickle cell disease (SCD), specifically, Hb polymerization and red blood cell sickling. Several such compounds are currently being clinically studied for the treatment of SCD. Based on the previously reported non-covalent Hb binding characteristics of substituted aryloxyalkanoic acids that exhibited antisickling properties, we designed, synthesized and evaluated 18 new compounds (KAUS II series) for enhanced antisickling activities. Surprisingly, select test compounds showed no antisickling effects or promoted erythrocyte sickling. Additionally, the compounds showed no significant effect on Hb oxygen affinity (or in some cases, even decreased the affinity for oxygen). The X-ray structure of deoxygenated Hb in complex with a prototype compound, KAUS-23, revealed that the effector bound in the central water cavity of the protein, providing atomic level explanations for the observed functional and biological activities. Although the structural modification did not lead to the anticipated biological effects, the findings provide important direction for designing candidate antisickling agents, as well as a framework for novel Hb allosteric effectors that conversely, decrease the protein affinity for oxygen for potential therapeutic use for hypoxic- and/or ischemic-related diseases. [ABSTRACT FROM AUTHOR]

Published
2016
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30. Theonellamide G, a Potent Antifungal and Cytotoxic Bicyclic Glycopeptide from the Red Sea Marine Sponge Theonella swinhoei.

Author

Youssef, Diaa T. A., Shaala, Lamiaa A., Mohamed, Gamal A., Badr, Jihan M., Bamanie, Faida H., and Ibrahim, Sabrin R. M.

Abstract

In our search for bioactive metabolites from marine organisms, we have investigated the polar fraction of the organic extract of the Red Sea sponge Theonella swinhoei. Successive chromatographic separations and final HPLC purification of the potent antifungal fraction afforded a new bicyclic glycopeptide, theonellamide G (1). The structure of the peptide was determined using extensive 1D and 2D NMR and high-resolution mass spectral determinations. The absolute configuration of theonellamide G was determined by chemical degradation and 2D NMR spectroscopy. Theonellamide G showed potent antifungal activity towards wild and amphotericin B-resistant strains of Candida albicans with IC50 of 4.49 and 2.0 μM, respectively. Additionally, it displayed cytotoxic activity against the human colon adenocarcinoma cell line (HCT-16) with IC50 of 6.0 μM. These findings provide further insight into the chemical diversity and biological activities of this class of compounds. [ABSTRACT FROM AUTHOR]

Published
2014
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31. Modelling, Control Strategy of DFIG in a Wind Energy System and Feasibility Study of a Wind Farm in Morocco.

Author

Faida, H. and Saadi, J.

Subjects
WIND energy conversion systems, ELECTRIC generators, WIND power plants
Abstract

In this work, our goal in the first time is to control a generator in a wind system to improve its performance. Thus, we chose to model the DFIG for its performance in wind systems, we chose the type of command to implement it and finally the block diagram of the system to regulate. Indeed, the control strategy chosen for the DFIG is a vector control in an active power and reactive stator. The equation, the choice of Landmark two-phase and simplifications necessary for the synthesis of controllers is presented. And a simulation in MATLAB 7 is made in this sense. Secondly, this work is the result of a feasibility study project of electricity generation through wind turbines (WTG). In fact, we analyzed the wind data collected during one year at a site in Morocco. We assessed all graphs that are the basis for achieving the final goal: namely the potential wind site, the Weibull distribution of wind frequencies, analysis of calm wind and diurnal variation, the prediction of energy based on a judicious choice of the machine and the determination of wind direction for implementation of wind turbines. Subsequently, we studied the impact of wind integration on the grid at the point of common coupling, and we proposed an industrial solution for remote management to optimize the exploitation of the production of this wind farm. [ABSTRACT FROM AUTHOR]

Published
2010

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