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4. Natural products in drug discovery: advances and opportunities

Author

Atanasov, A. G., Zotchev, S. B., Dirsch, V. M., Orhan, I. E., Banach, M., Rollinger, J. M., Barreca, D., Weckwerth, W., Bauer, R., Bayer, E. A., Majeed, M., Bishayee, A., Bochkov, V., Bonn, G. K., Braidy, N., Bucar, F., Cifuentes, A., D'Onofrio, G., Bodkin, M., Diederich, M., Dinkova-Kostova, A. T., Efferth, T., El Bairi, K., Arkells, N., Fan, T. -P., Fiebich, B. L., Freissmuth, M., Georgiev, M. I., Gibbons, S., Godfrey, K. M., Gruber, C. W., Heer, J., Huber, L. A., Ibanez, E., Kijjoa, A., Kiss, A. K., Lu, A., Macias, F. A., Miller, M. J. S., Mocan, A., Muller, R., Nicoletti, F., Perry, G., Pittala, V., Rastrelli, L., Ristow, M., Russo, G. L., Silva, A. S., Schuster, D., Sheridan, H., Skalicka-Wozniak, K., Skaltsounis, L., Sobarzo-Sanchez, E., Bredt, D. S., Stuppner, H., Sureda, A., Tzvetkov, N. T., Vacca, R. A., Aggarwal, B. B., Battino, M., Giampieri, F., Wink, M., Wolfender, J. -L., Xiao, J., Yeung, A. W. K., Lizard, G., Popp, M. A., Heinrich, M., Berindan-Neagoe, I., Stadler, M., Daglia, M., Verpoorte, R., Supuran, C. T., Ministerio de Economía y Competitividad (España), Agencia Estatal de Investigación (España), Ministerio de Ciencia, Innovación y Universidades (España), Atanasov, A. G., Zotchev, S. B., Dirsch, V. M., Orhan, I. E., Banach, M., Rollinger, J. M., Barreca, D., Weckwerth, W., Bauer, R., Bayer, E. A., Majeed, M., Bishayee, A., Bochkov, V., Bonn, G. K., Braidy, N., Bucar, F., Cifuentes, A., D'Onofrio, G., Bodkin, M., Diederich, M., Dinkova-Kostova, A. T., Efferth, T., El Bairi, K., Arkells, N., Fan, T. -P., Fiebich, B. L., Freissmuth, M., Georgiev, M. I., Gibbons, S., Godfrey, K. M., Gruber, C. W., Heer, J., Huber, L. A., Ibanez, E., Kijjoa, A., Kiss, A. K., Lu, A., Macias, F. A., Miller, M. J. S., Mocan, A., Muller, R., Nicoletti, F., Perry, G., Pittala, V., Rastrelli, L., Ristow, M., Russo, G. L., Silva, A. S., Schuster, D., Sheridan, H., Skalicka-Wozniak, K., Skaltsounis, L., Sobarzo-Sanchez, E., Bredt, D. S., Stuppner, H., Sureda, A., Tzvetkov, N. T., Vacca, R. A., Aggarwal, B. B., Battino, M., Giampieri, F., Wink, M., Wolfender, J. -L., Xiao, J., Yeung, A. W. K., Lizard, G., Popp, M. A., Heinrich, M., Berindan-Neagoe, I., Stadler, M., Daglia, M., Verpoorte, R., and Supuran, C. T.

Subjects
0301 basic medicine, Engineering, Drug Industry, Review Article, Communicable Diseases, Natural (archaeology), 03 medical and health sciences, 0302 clinical medicine, Transferases, Neoplasms, Drug Discovery, Humans, Pharmaceutical industry, Pharmacology, Biological Products, Natural products, Genome, business.industry, Drug discovery, General Medicine, Chemical biology, 030104 developmental biology, Risk analysis (engineering), 030220 oncology & carcinogenesis, Genome mining, business
Abstract

The International Natural Product Sciences Taskforce: et al., Natural products and their structural analogues have historically made a major contribution to pharmacotherapy, especially for cancer and infectious diseases. Nevertheless, natural products also present challenges for drug discovery, such as technical barriers to screening, isolation, characterization and optimization, which contributed to a decline in their pursuit by the pharmaceutical industry from the 1990s onwards. In recent years, several technological and scientific developments — including improved analytical tools, genome mining and engineering strategies, and microbial culturing advances — are addressing such challenges and opening up new opportunities. Consequently, interest in natural products as drug leads is being revitalized, particularly for tackling antimicrobial resistance. Here, we summarize recent technological developments that are enabling natural product-based drug discovery, highlight selected applications and discuss key opportunities., A.C. and E.I. thank the Ministerio de Ciencia, Innovación y Universidades, Spain (Project AGL2017-89417-R) for support. F.A.M. acknowledges the support by Ministerio de Economia y Competitividad, Spain (project AGL2017-88083-R).

Published
2021
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5. Toxicity evaluation of sulfamides and coumarins that efficiently inhibit human carbonic anhydrases

Author

Aspatwar, A., Berrino, E., Bua, S., Carta, F., Capasso, C., Parkkila, S., and Supuran, C. T.

Subjects
Sulfonamides, carbonic anhydrases, animal structures, Dose-Response Relationship, Drug, Molecular Structure, Brief Report, fungi, Carbonic anhydrases, inhibitors, toxicity screening, zebrafish, RM1-950, Structure-Activity Relationship, Coumarins, Animals, Humans, Therapeutics. Pharmacology, Carbonic Anhydrase Inhibitors
Abstract

Here, we report a toxicity study, conducted on zebrafish larvae, of a series of coumarin and sulfamide compounds that were previously reported as inhibitors of human (h) metalloenzymes, carbonic anhydrases (CAs, EC 4.2.1.1). Due to the high relevance of hCA inhibitors as theragnostic agents, it is of pivotal importance to address safety issues that may arise from the initial in vivo toxicological assessment using zebrafish, a relevant model for biomedical research. None of the reported compounds showed adverse phenotypic effects or tissue damage on developing zebrafish larvae after 5 days of exposure. Our study suggests that the coumarin and sulfamide derivatives considered here are safe and suitable for further development and testing.

Published
2020
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10. Activation studies of the γ-carbonic anhydrases from the antarctic marine bacteria pseudoalteromonas haloplanktis and colwellia psychrerythraea with amino acids and amines

Author

Angeli, A., Del Prete, S., Osman, S. M., AlOthman, Z., Donald, W. A., Capasso, C., and Supuran, C. T.

Subjects
Activator, Amine, Amino acid, Antarctic bacteria, Carbonic anhydrase, Colwellia psychrerythraea, Metalloenzymes, Pseudoalteromonas haloplanktis, Alteromonadaceae, Amines, Amino Acids, Antarctic Regions, Aquatic Organisms, Carbonic Anhydrases, Kinetics, Metabolic Networks and Pathways, Pseudoalteromonas, Structure-Activity Relationship
Published
2019

14. Carbonic anhydrase inhibitors as novel drugs against mycobacterial β-carbonic anhydrases: An update on in vitro and in vivo studies

Author

Aspatwar, A., Winum, J. -Y., Carta, F., Supuran, C. T., Hammaren, M., Parikka, M., and Parkkila, S.

Subjects
Carbonic anhydrase inhibitors, Drug targets, In vitro inhibition, In vivo inhibition, Mycobacterial diseases, Mycobacterium tuberculosis, Β-carbonic anhydrases, Antitubercular Agents, Bacterial Proteins, Biofilms, Carbonic Anhydrase I, Carbonic Anhydrase Inhibitors, Models, Molecular, Structure-Activity Relationship, Virulence, bacterial infections and mycoses
Published
2018

16. The interactome of metabolic enzyme carbonic anhydrase IX reveals novel roles in tumor cell migration and invadopodia/MMP14-mediated invasion

Author

Swayampakula, M, primary, McDonald, P C, additional, Vallejo, M, additional, Coyaud, E, additional, Chafe, S C, additional, Westerback, A, additional, Venkateswaran, G, additional, Shankar, J, additional, Gao, G, additional, Laurent, E M N, additional, Lou, Y, additional, Bennewith, K L, additional, Supuran, C T, additional, Nabi, I R, additional, Raught, B, additional, and Dedhar, S, additional

Published
2017
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18. Carbonic anhydrase inhibitors: the X-ray crystal structure of ethoxzolamide complexed to human isoform II reveals the importance of Thr200 and Gln92 for obtaining tight-binding inhibitors

Author

Di Fiore A., Antel J., Waldeck H., Witte A., Wurl M., Scozzafava A., Supuran C. T., De Simone G., PEDONE, CARLO, Di Fiore, A., Pedone, Carlo, Antel, J., Waldeck, H., Witte, A., Wurl, M., Scozzafava, A., Supuran, C. T., and De Simone, G.

Abstract

Ethoxzolamide, an almost forgotten inhibitor of the metalloenzyme carbonic anhydrase (CA, EC 4.2.1.1), is the only classical inhibitor whose structure in adduct with any isoform was not reported yet. We report here the inhibition data of this molecule with the 12 catalytically active mammalian isozymes (CA I-CA XIV) and the X-ray crystal structure with the cytosolic, ubiquitous isoform CA II. These data are presumably useful for the design of novel CA inhibitors, targeting various CA isozymes, considering that ethoxzolamide was already the lead molecule to obtain the second generation inhibitors, dorzolamide and brinzolamide, clinically used antiglaucoma agents with topical action, as well as various other investigational agents.

Published
2008

23. A Divalent PAMAM-Based Matrix Metalloproteinase/Carbonic Anhydrase Inhibitor for the Treatment of Dry Eye Syndrome

Author

Richichi, B., primary, Baldoneschi, V., additional, Burgalassi, S., additional, Fragai, M., additional, Vullo, D., additional, Akdemir, A., additional, Dragoni, E., additional, Louka, A., additional, Mamusa, M., additional, Monti, D., additional, Berti, D., additional, Novellino, E., additional, Rosa, G. De, additional, Supuran, C. T., additional, and Nativi, C., additional

Published
2015
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24. Taking advantage of tumor cell adaptations to hypoxia for developing new tumor markers and treatment strategies

Author

Ebbesen, P, Pettersen, E O, Gorr, T A, Jobst, G, Williams, K, Kieninger, J, Wenger, R H, Pastorekova, S, Dubois, L, Lambin, P, Wouters, B G, Van den Beucken, T, Beucken, D, Supuran, C T, Poellinger, L, Ratcliffe, P, Kanopka, A, Görlach, A, Gassmann, M, Harris, A L, Maxwell, P, Scozzafava, A, University of Zurich, and Ebbesen, P

Subjects
3004 Pharmacology, 10076 Center for Integrative Human Physiology, 3002 Drug Discovery, 570 Life sciences, biology, 610 Medicine & health, 10081 Institute of Veterinary Physiology, 10052 Institute of Physiology
Published
2009
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28. Characterization of the first beta-class carbonic anhydrase from an arthropod (Drosophila melanogaster) and phylogenetic analysis of beta-class carbonic anhydrases in invertebrates

Author

Syrjänen, L, Tolvanen, M, Hilvo, M, Olatubosun, A, Innocenti, A, Scozzafava, A, Leppiniemi, J, Niederhauser, B, Hytönen, V P, Gorr, T A, Parkkila, S, Supuran, C T, Syrjänen, L, Tolvanen, M, Hilvo, M, Olatubosun, A, Innocenti, A, Scozzafava, A, Leppiniemi, J, Niederhauser, B, Hytönen, V P, Gorr, T A, Parkkila, S, and Supuran, C T

Abstract

BACKGROUND: The beta-carbonic anhydrase (CA, EC 4.2.1.1) enzymes have been reported in a variety of organisms, but their existence in animals has been unclear. The purpose of the present study was to perform extensive sequence analysis to show that the beta-CAs are present in invertebrates and to clone and characterize a member of this enzyme family from a representative model organism of the animal kingdom, e.g., Drosophila melanogaster. RESULTS: The novel beta-CA gene, here named DmBCA, was identified from FlyBase, and its orthologs were searched and reconstructed from sequence databases, confirming the presence of beta-CA sequences in 55 metazoan species. The corresponding recombinant enzyme was produced in Sf9 insect cells, purified, kinetically characterized, and its inhibition was investigated with a series of simple, inorganic anions. Holoenzyme molecular mass was defined by dynamic light scattering analysis and gel filtration, and the results suggested that the holoenzyme is a dimer. Double immunostaining confirmed predictions based on sequence analysis and localized DmBCA protein to mitochondria. The enzyme showed high CO2 hydratase activity, with a kcat of 9.5 x 105 s-1 and a kcat/KM of 1.1 x 108 M-1s-1. DmBCA was appreciably inhibited by the clinically-used sulfonamide acetazolamide, with an inhibition constant of 49 nM. It was moderately inhibited by halides, pseudohalides, hydrogen sulfide, bisulfite and sulfate (KI values of 0.67 - 1.36 mM) and more potently by sulfamide (KI of 0.15 mM). Bicarbonate, nitrate, nitrite and phenylarsonic/boronic acids were much weaker inhibitors (KIs of 26.9 - 43.7 mM). CONCLUSIONS: The Drosophila beta-CA represents a highly active mitochondrial enzyme that is a potential model enzyme for anti-parasitic drug development.

Published
2010

43. A Divalent PAMAM-Based Matrix Metalloproteinase/Carbonic Anhydrase Inhibitor for the Treatment of Dry Eye Syndrome.

Author

Richichi, B., Baldoneschi, V., Burgalassi, S., Fragai, M., Vullo, D., Akdemir, A., Dragoni, E., Louka, A., Mamusa, M., Monti, D., Berti, D., Novellino, E., Rosa, G. De, Supuran, C. T., and Nativi, C.

Subjects
AMIDE derivatives, MATRIX metalloproteinase inhibitors, DRUG delivery systems, SULFONAMIDES, CHEMICAL synthesis, CARBONIC anhydrase
Abstract

Synthetic sulfonamide derivatives are a class of potent matrix metalloproteinase inhibitors (MMPI) that have potential for the treatment of diseases related to uncontrolled expression of these enzymes. The lack of selectivity of the large majority of such inhibitors, leading to the inhibition of MMPs in tissues other than the targeted one, has dramatically reduced the therapeutic interest in MMPIs. The recent development of efficient drug delivery systems that allow the transportation of a selected drug to its site of action has opened the way to new perspectives in the use of MMPIs. Here, a PAMAM-based divalent dendron with two sulfonamidic residues was synthesized. This nanomolar inhibitor binds to the catalytic domain of two MMPs as well as to the transmembrane human carbonic anhydrases (hCAs) XII, which is present in the eye and considered an antiglaucoma target. In the animal model of an experimental dry eye, no occurrence of dotted staining in eyes treated with our inhibitor was observed, indicating no symptoms of corneal desiccation. [ABSTRACT FROM AUTHOR]

Published
2016
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