16 results on '"Shahbaz Shamim"'
Search Results
2. N‑Aryl-3,4-dihydroisoquinoline Carbothioamide Analogues as Potential Urease Inhibitors
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Fayaz Ali, Shahbaz Shamim, Mehreen Lateef, Khalid Mohammed Khan, Muhammad Taha, Uzma Salar, Abdul Wadood, Ashfaq Ur Rehman, Noor Ul Ain Nawaz, and Shahnaz Perveen
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Chemistry ,QD1-999 - Published
- 2021
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3. Perplexing Polyphenolics: The Isolations, Syntheses, Reappraisals, and Bioactivities of Flavonoids, Isoflavonoids, and Neoflavonoids from 2016 to 2022
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Syed Muhammad Umer, Shahbaz Shamim, Khalid Mohammed Khan, and Rahman Shah Zaib Saleem
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flavonoids ,isoflavonoids ,neoflavonoids ,total synthesis ,semisynthesis ,bioactivities ,Science - Abstract
Flavonoids, isoflavonoids, neoflavonoids, and their various subcategories are polyphenolics–an extensive class of natural products. These compounds are bioactive and display multiple activities, including anticancer, antibacterial, antiviral, antioxidant, and neuroprotective activities. Thus, these compounds can serve as leads for therapeutic agents or targets for complex synthesis; they are coveted and routinely isolated, characterized, biologically evaluated, and synthesized. However, data regarding the compounds’ sources, isolation procedures, structural novelties, bioactivities, and synthetic schemes are often dispersed and complex, a dilemma this review aims to address. To serve as an easily accessible guide for researchers wanting to apprise themselves of the latest advancements in this subfield, this review summarizes seventy-six (76) articles published between 2016 and 2022 that detail the isolation and characterization of two hundred and forty-nine (249) novel compounds, the total and semisyntheses of thirteen (13) compounds, and reappraisals of the structures of twenty (20) previously reported compounds and their bioactivities. This article also discusses new synthetic methods and enzymes capable of producing or modifying flavonoids, isoflavonoids, or neoflavonoids.
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- 2023
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4. The Synthesis and Chemistry of Quinolinediones and their Carbocyclic Analogs
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Eboh Monday Odin, Abdul Hameed, Uchechukwu C. Okoro, Khalid Mohammed Khan, Shahbaz Shamim, Shafia Iftekhar, Efeturi A. Onoabedje, Irfan Ali, and Samuel A. Egu
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Chemistry ,Organic Chemistry ,Organic chemistry - Abstract
Abstract: Quinoline-5,8-dione and naphthoquinone nuclei are very important substructures in industrial chemicals and pharmaceuticals. These compounds exhibit a wide variety of activities, including antifungal, antibacterial, antimalarial, antineoplastic, anticoagulant, anticancer, antiviral, radical scavenging, antiplatelet, trypanocidal, cytotoxic, and antineoplastic activities. Currently, several research articles on the importance of many natural and synthetic drugs containing quinolinequinone have been reported. This review covers the progress in quinolinequinone and naphthoquinone chemistry over the last five decades.
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- 2022
5. 2‐Mercapto Benzoxazole Derivatives as Novel Leads: Urease Inhibition, In Vitro and In Silico Studies
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Ashfaq Ur Rehman, Uzma Salar, Shahnaz Perveen, Mehreen Lateef, Shahbaz Shamim, Dorcas Olufunke Moronkola, Muhammad Taha, Fazal Rahim, I. A. Oladosu, Abdul Wadood, Modinat M. Balogun, and Khalid Mohammed Khan
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chemistry.chemical_compound ,Urease enzyme ,Urease ,biology ,Biochemistry ,Drug discovery ,Chemistry ,In silico ,biology.protein ,General Chemistry ,Benzoxazole ,In vitro - Published
- 2021
6. Substituted Benzimidazole Analogues as Potential α-Amylase Inhibitors and Radical Scavengers
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Kanwal, Saurabh Bhatia, Shahnaz Perveen, Akinsola Akande, Sherifat A. Aboaba, Muhammad Taha, Sridevi Chigurupati, Uzma Salar, Shahbaz Shamim, Khalid Mohammed Khan, Muhammad Riaz, Abdul Wadood, and Shazia Syed
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chemistry.chemical_classification ,Benzimidazole ,Antioxidant ,ABTS ,DPPH ,General Chemical Engineering ,medicine.medical_treatment ,General Chemistry ,Ascorbic acid ,Article ,Chemistry ,chemistry.chemical_compound ,Enzyme ,chemistry ,medicine ,QD1-999 ,IC50 ,Nuclear chemistry ,Acarbose ,medicine.drug - Abstract
Benzimidazole scaffolds are known to have a diverse range of biological activities and found to be antidiabetic and antioxidant. In this study, a variety of arylated benzimidazoles 1–31 were synthesized. Except for compounds 1, 6, 7, and 8, all are new derivatives. All compounds were screened for α-amylase inhibitory, 2,2′-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), and 2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activities. In vitro screening results revealed that all molecules demonstrated significant α-amylase inhibition with IC50 values of 1.86 ± 0.08 to 3.16 ± 0.31 μM as compared to standard acarbose (IC50 = 1.46 ± 0.26 μM). However, compounds showed significant ABTS and DPPH radical scavenging potentials with IC50 values in the range of 1.37 ± 0.21 to 4.00 ± 0.10 μM for ABTS and 1.36 ± 0.09 to 3.60 ± 0.20 μM for DPPH radical scavenging activities when compared to ascorbic acid with IC50 values of 0.72 ± 0.21 and 0.73 ± 0.05 μM for ABTS and DPPH radical scavenging potentials, respectively. Structure–activity relationship (SAR) was established after critical analysis of varying substitution effects on α-amylase inhibitory and radical scavenging (ABTS and DPPH) potentials. However, molecular docking was also performed to figure out the active participation of different groups of synthetic molecules during binding with the active pocket of the α-amylase enzyme.
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- 2021
7. N‑Aryl-3,4-dihydroisoquinoline Carbothioamide Analogues as Potential Urease Inhibitors
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Noor Ul Ain Nawaz, Mehreen Lateef, Shahbaz Shamim, Fayaz Ali, Khalid Mohammed Khan, Abdul Wadood, Muhammad Taha, Uzma Salar, Ashfaq Ur Rehman, and Shahnaz Perveen
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Inhibitory potential ,Urease ,biology ,Stereochemistry ,Hydrogen bond ,General Chemical Engineering ,Aryl ,General Chemistry ,In vitro ,Article ,chemistry.chemical_compound ,Chemistry ,Thiourea ,chemistry ,Urease Inhibitors ,biology.protein ,IC50 ,QD1-999 - Abstract
N-Aryl-3,4-dihydroisoquinoline carbothioamide analogues 1-22 were synthesized by a simple one-step reaction protocol and subjected to in vitro urease inhibition studies for the first time. All compounds 1-22 were found active and showed significant to moderate urease inhibitory potential. Specifically, analogues 1, 2, 4, and 7 were identified to be more potent (IC50 = 11.2 ± 0.81-20.4 ± 0.22 μM) than the standard thiourea (IC50 = 21.7 ± 0.34 μM). The structure-activity relationship showed that compounds bearing electron-donating groups showed superior activity. Molecular docking study on the most active derivatives revealed a good protein-ligand interaction profile against the corresponding target with key interactions, including hydrogen bonding, hydrophobic, and π-anion interactions.
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- 2021
8. Synthesis, in vitro, and in silico studies of newly functionalized quinazolinone analogs for the identification of potent α-glucosidase inhibitors
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Shahbaz Shamim, Mohammad Mahdavi, Mohammad Ali Faramarzi, Bagher Larijani, Hayat Wali, Muhammad Taha, Uzma Salar, Ayaz Anwar, Shahnaz Perveen, and Khalid Mohammed Khan
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chemistry.chemical_classification ,biology ,010405 organic chemistry ,Stereochemistry ,Phenyl isothiocyanate ,Active site ,General Chemistry ,010402 general chemistry ,01 natural sciences ,In vitro ,0104 chemical sciences ,chemistry.chemical_compound ,Enzyme ,chemistry ,biology.protein ,Anthranilic acid ,medicine ,Quinazolinone ,Triethylamine ,Acarbose ,medicine.drug - Abstract
Functionalized quinazolinone derivatives 1–30 were synthesized by two-step reaction. First, anthranilic acid was treated with substituted phenyl isothiocyanate to synthesize 3-aryl-2-thioxo-2,3-dihydroquinazolinone derivatives 1–8 which in turn reacted with different bromoacetophenone derivatives to obtain fully functionalized quinazolinone derivatives 9–30. Both reactions were catalyzed by triethylamine. All the products were characterized by EI-, HREI-MS, 1H-, and 13CNMR spectroscopic techniques. All compounds were subjected to their in vitro α-glucosidase inhibitory activity. Results showed that except compound 1–3, 5, 7, and 22, all compounds were found potent and showed many folds increased α-glucosidase enzyme inhibition as compared to standard acarbose (IC50 = 750.0 ± 10.0 µM). Compound 13 (IC50 = 85.0 ± 0.5 µM) was recognized as the most potent analog of the whole series, with ninefold enhanced inhibitory potential than the standard acarbose. Compounds 1–9, 11, 12, 22, and 26 were structurally known compounds, while remaining all are new. Kinetic study on compound 13 showed that the compound is following a competitive-type inhibition mechanism. Furthermore, in silico studies have also been performed to better rationalize the interactions between synthetic compound and active site of the enzyme.
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- 2021
9. Dihydropyrimidones: A ligands urease recognition study and mechanistic insight through in vitro and in silico approach
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Sahib Gul Afridi, Farman Ali Khan, Khalid Mohammed Khan, Shahnaz Perveen, Shahbaz Shamim, Kanwal, Ajmal Khan, Farman Ali, Muhammad Arif Lodhi, and Nisar Ullah
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biology ,Urease ,010405 organic chemistry ,Chemistry ,Stereochemistry ,In silico ,Organic Chemistry ,Active site ,01 natural sciences ,In vitro ,0104 chemical sciences ,010404 medicinal & biomolecular chemistry ,chemistry.chemical_compound ,Docking (molecular) ,biology.protein ,Urea ,Bioorganic chemistry ,General Pharmacology, Toxicology and Pharmaceutics ,Cytotoxicity - Abstract
Scaffold varied dihydropyrimidone derivatives 1–20 were evaluated for their selective urease inhibitory kinetics potential. Compounds 1, 2, 3, 4, 5, 6, and 12 were found to be the most promising urease inhibitors and showed the inhibition (Ki values) within the range of 9.9 ± 0.5 to 18.3 ± 0.4 µM. Lineweaver–Burk plot, Dixon plot and their secondary replots confirm that all these molecules have followed competitive mode of inhibition. Docking arrangements (MOE) revealed that all the ligands bind in the active site and therefore compete with substrate urea. Molecular docking studies of all compounds have confirmed the binding interactions of various ligands with the amino acid residues as well as Ni atoms of active site. Furthermore, these compounds 1–20 were also tested for their cytotoxicity against human neutrophils and plants and were found to be non-toxic.
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- 2020
10. Synthesis and screening of (E)-3-(2-benzylidenehydrazinyl)-5,6-diphenyl-1,2,4-triazine analogs as novel dual inhibitors of α-amylase and α-glucosidase
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Ashfaq Ur Rehman, Muhammad Taha, Muhammad Ali, Khalid Mohammed Khan, Shahbaz Shamim, Shahnaz Perveen, Ahmad Alhowail, Sridevi Chigurupati, Uzma Salar, Abdul Wadood, and Nisar Ullah
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Molecular model ,Stereochemistry ,Kinetics ,01 natural sciences ,Biochemistry ,chemistry.chemical_compound ,Structure-Activity Relationship ,Drug Discovery ,medicine ,Structure–activity relationship ,Humans ,Amylase ,Molecular Biology ,Triazine ,Acarbose ,chemistry.chemical_classification ,biology ,Molecular Structure ,010405 organic chemistry ,Chemistry ,Triazines ,Organic Chemistry ,alpha-Glucosidases ,In vitro ,0104 chemical sciences ,Molecular Docking Simulation ,010404 medicinal & biomolecular chemistry ,Enzyme ,Diabetes Mellitus, Type 2 ,biology.protein ,alpha-Amylases ,medicine.drug - Abstract
(E)-3-(2-Benzylidenehydrazinyl)-5,6-diphenyl-1,2,4-triazines analogs 1–27 were synthesized by multi-step reaction scheme and subjected to in vitro inhibitory screening against α-amylase and α-glucosidase enzymes. Out of these twenty-seven synthetic analogs, ten compounds 14–17, 19, and 21–25 are structurally new. All compounds exhibited good to moderate inhibitory potential in terms of IC50 values ranging (IC50 = 13.02 ± 0.04–46.90 ± 0.05 µM) and (IC50 = 13.09 ± 0.08–46.44 ± 0.24 µM) in comparison to standard acarbose (IC50 = 12.94 ± 0.27 µM and 10.95 ± 0.08 µM), for α-amylase and α-glucosidase, respectively. Structure-activity relationship indicated that analogs with halogen substitution(s) were found more active as compared to compounds bearing other substituents. Kinetic studies on most active α-amylase and α-glucosidase inhibitors 5, 7, 9, 15, 24, and 27, suggested non-competitive and competitive types of inhibition mechanism for α-amylase and α-glucosidase, respectively. Molecular docking studies predicted the good protein-ligand interaction (PLI) profile with key interactions such as arene-arene, H
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- 2020
11. Syntheses, in vitro α-amylase and α-glucosidase dual inhibitory activities of 4-amino-1,2,4-triazole derivatives their molecular docking and kinetic studies
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Kanwal, Muhammad Taha, Ashfaq Ur Rehman, Shahnaz Perveen, Khalid Mohammed Khan, Sridevi Chigurupati, Abdul Wadood, Emmanuel Oloruntoba Yeye, Shahbaz Shamim, Sherifat A. Aboaba, Mari Kannan Maharajan, and Shehryar Hameed
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Stereochemistry ,In silico ,Clinical Biochemistry ,Triazole ,Pharmaceutical Science ,Biochemistry ,chemistry.chemical_compound ,Structure-Activity Relationship ,Drug Discovery ,Animals ,Glycoside Hydrolase Inhibitors ,Amylase ,Molecular Biology ,chemistry.chemical_classification ,biology ,Dose-Response Relationship, Drug ,Molecular Structure ,Aryl ,Organic Chemistry ,1,2,4-Triazole ,alpha-Glucosidases ,Triazoles ,In vitro ,Rats ,Molecular Docking Simulation ,Kinetics ,Enzyme ,chemistry ,biology.protein ,Proton NMR ,Molecular Medicine ,alpha-Amylases - Abstract
Thirty-three 4-amino-1,2,4-triazole derivatives 1–33 were synthesized by reacting 4-amino-1,2,4-triazole with a variety of benzaldehydes. The synthetic molecules were characterized via 1H NMR and EI-MS spectroscopic techniques and evaluated for their anti-hyperglycemic potential. Compounds 1–33 exhibited good to moderate in vitro α-amylase and α-glucosidase inhibitory activities in the range of IC50 values 2.01 ± 0.03–6.44 ± 0.16 and 2.09 ± 0.08–6.54 ± 0.10 µM as compared to the standard acarbose (IC50 = 1.92 ± 0.17 µM) and (IC50 = 1.99 ± 0.07 µM), respectively. The limited structure-activity relationship suggested that different substitutions on aryl part of the synthetic compounds are responsible for variable activity. Kinetic study predicted that compounds 1–33 followed mixed and non-competitive type of inhibitions against α-amylase and α-glucosidase enzymes, respectively. In silico studies revealed that both triazole and aryl ring along with different substitutions were playing an important role in the binding interactions of inhibitors within the enzyme pocket. The synthetic molecules were found to have dual inhibitory potential against both enzymes thus they may serve as lead candidates for the drug development and research in the future studies.
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- 2019
12. Synthesis, in vitro $$\alpha $$ α -glucosidase inhibitory activity, and in silico study of (E)-thiosemicarbazones and (E)-2-(2-(arylmethylene)hydrazinyl)-4-arylthiazole derivatives
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Basharat Ali, Shahnaz Perveen, Sujhla Hamid, Muhammad Riaz, Khalid Mohammed Khan, Uzma Salar, Shahbaz Shamim, Muhammad Taha, Abdul Wadood, Farman Ali, Mohammed Ashraf, and Muhammad Ali
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Molecular model ,Stereochemistry ,In silico ,Alpha (ethology) ,010402 general chemistry ,01 natural sciences ,Catalysis ,Inorganic Chemistry ,chemistry.chemical_compound ,Drug Discovery ,Physical and Theoretical Chemistry ,Thiazole ,Molecular Biology ,α glucosidase inhibitory ,chemistry.chemical_classification ,biology ,010405 organic chemistry ,Organic Chemistry ,Active site ,General Medicine ,In vitro ,0104 chemical sciences ,Enzyme ,chemistry ,biology.protein ,Information Systems - Abstract
This study is focused on the identification of thiazole-based inhibitors for the $$\alpha $$ -glucosidase enzyme. For that purpose, (E)-2-(2-(arylmethylene)hydrazinyl)-4-arylthiazole derivatives were synthesized in two steps and characterized by various spectroscopic techniques. All derivatives and intermediates were evaluated for their in vitro $$\alpha $$ -glucosidase inhibitory activity. Thiosemicarbazones 20 and 35, and cyclized thiazole derivatives 2, 5–11, 13, 15, 21–24, 27–31, and 36–37 showed significant inhibitory potential in the range of $$\hbox {IC}_{50}=6.2\pm 0.19$$ – $$43.6\pm 0.23~\upmu \hbox {M}$$ as compared to standard acarbose ( $$\hbox {IC}_{50}=37.7\pm 0.19~\upmu \hbox {M}$$ ). A molecular modeling study was carried out to understand the binding interactions of compounds with the active site of enzyme.
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- 2018
13. Synthesis, in vitro, and in silico evaluation of Indazole Schiff bases as potential α-glucosidase inhibitors
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Mohammad Ali Faramarzi, Shahnaz Perveen, Bagher Larijani, Khalid Mohammed Khan, Bushra, Rafaila Rafique, Nisar Ullah, Muhammad Taha, Mohammad Mahdavi, Shahbaz Shamim, and Uzma Salar
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chemistry.chemical_classification ,Indazole ,Schiff base ,biology ,Stereochemistry ,In silico ,Organic Chemistry ,Active site ,Analytical Chemistry ,Inorganic Chemistry ,chemistry.chemical_compound ,Enzyme ,Non-competitive inhibition ,chemistry ,biology.protein ,Moiety ,Structure–activity relationship ,Spectroscopy - Abstract
Indazole Schiff bases were synthesized 1–24 and structurally characterized by different spectroscopic techniques such as EI-MS, HREI-MS, 1H- and 13C-NMR. Stereochemistry of azomethine moiety in synthesized compounds was confirmed by 2D-NOESY. Among the twenty-four compounds, fourteen compounds 1–5, 7, 9–14, 17, and 20 are structurally new. Compounds 1–24 were screened for in vitro α-glucosidase enzyme inhibitory activity. All compounds were In vitro α-glucosidase inhibitory assay results identified a number of molecules including 1, 2, 4, 7, 9, 10, 12, 13, 18, 19, 21, and 23 as potent α-glucosidase inhibitors with IC50 values 9.4 ± 0.1 to 303.7 ± 0.1 μM as compared to the standard acarbose (IC50 = 750 ± 10 µM). Compound 1 (IC50 = 9.43 ± 0.1 µM) was found to be the most potent molecule of this library. Kinetic studies on most active compound 1 suggested the competitive inhibition mechanism. In silico studies indicated the interaction details between analogs (ligands) and active site of α-glucosidase enzyme.
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- 2021
14. Dihydropyridines as potential α-amylase and α-glucosidase inhibitors: Synthesis, in vitro and in silico studies
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Kanwal, Khalid Mohammed Khan, Sridevi Chigurupati, Muhammad Taha, Muhammad Naseem Khan, Shehryar Hameed, Shahbaz Shamim, Minhajul Arfeen, and Hina Yousuf
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Dihydropyridines ,Stereochemistry ,In silico ,In Vitro Techniques ,01 natural sciences ,Biochemistry ,Structure-Activity Relationship ,Drug Discovery ,medicine ,Molecule ,Computer Simulation ,Glycoside Hydrolase Inhibitors ,Amylase ,Enzyme Inhibitors ,Molecular Biology ,Acarbose ,chemistry.chemical_classification ,biology ,010405 organic chemistry ,Chemistry ,Spectrum Analysis ,Organic Chemistry ,Dihydropyridine ,Carbon-13 NMR ,In vitro ,0104 chemical sciences ,010404 medicinal & biomolecular chemistry ,Enzyme ,biology.protein ,alpha-Amylases ,medicine.drug - Abstract
Dihydropyridine derivatives 1–31 were synthesized via one-pot solvent free condition and screened for in vitro against α-amylase and α-glucosidase enzyme. The synthetic derivatives 1–31 showed good α-amylase inhibition in the range of IC50 = 2.21 ± 0.06–9.97 ± 0.08 µM, as compared to the standard drug acarbose (IC50 = 2.01 ± 0.1 µM) and α-glucosidase inhibition in the range of IC50 = 2.31 ± 0.09–9.9 ± 0.1 µM as compared to standard acarbose (IC50 = 2.07 ± 0.1 µM), respectively. To determine the mode of binding interactions of synthetic molecules with active sites of enzyme, molecular docking studies were also performed. Different spectroscopic techniques such as 1H, 13C NMR, EI-MS, and HREI-MS were used to characterize all the synthetic compounds.
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- 2019
15. Synthesis, in vitro and in silico screening of 2-amino-4-aryl-6-(phenylthio) pyridine-3,5-dicarbonitriles as novel α-glucosidase inhibitors
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Muhammad Ali, Mohammad Mahdavi, Uzma Salar, Mohammad Ali Faramarzi, Bagher Larijani, Khalid Mohammed Khan, Shahnaz Perveen, Muhammad Taha, Shahbaz Shamim, and Abdul Jabbar
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Pyridines ,Stereochemistry ,In silico ,Saccharomyces cerevisiae ,01 natural sciences ,Biochemistry ,chemistry.chemical_compound ,Nitriles ,Drug Discovery ,Pyridine ,medicine ,Humans ,Structure–activity relationship ,Glycoside Hydrolase Inhibitors ,Molecular Biology ,Amination ,Acarbose ,chemistry.chemical_classification ,biology ,010405 organic chemistry ,Organic Chemistry ,Active site ,Ligand (biochemistry) ,In vitro ,0104 chemical sciences ,Molecular Docking Simulation ,010404 medicinal & biomolecular chemistry ,Enzyme ,Diabetes Mellitus, Type 2 ,chemistry ,Drug Design ,biology.protein ,medicine.drug - Abstract
Inhibition of α-glucosidase enzyme is of prime importance for the treatment of diabetes mellitus (DM). Apart of many organic scaffolds, pyridine based compounds have previously been reported for wide range of bioactivities. The current study reports a series of pyridine based synthetic analogues for their α-glucosidase inhibitory potential assessed by in vitro, kinetics and in silico studies. For this purpose, 2-amino-4-aryl-6-(phenylthio)pyridine-3,5-dicarbonitriles 1–28 were synthesized and subjected to in vitro screening. Several analogs, including 1–3, 7, 9, 11–14, and 16 showed many folds increased inhibitory potential in comparison to the standard acarbose (IC50 = 750 ± 10 µM). Interestingly, compound 7 (IC50 = 55.6 ± 0.3 µM) exhibited thirteen-folds greater inhibition strength than the standard acarbose. Kinetic studies on most potent molecule 7 revealed a competitive type inhibitory mechanism. In silico studies have been performed to examine the binding mode of ligand (compound 7) with the active site residues of α-glucosidase enzyme.
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- 2020
16. 5-Acetyl-6-methyl-4-aryl-3,4-dihydropyrimidin-2(1H)-ones: As potent urease inhibitors; synthesis, in vitro screening, and molecular modeling study
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Zaheer Ul-Haq, Muhammad Arif Lodhi, Farman Ali, Shahbaz Shamim, Muhammad Ali, Khalid Mohammed Khan, Uzma Salar, Shahnaz Perveen, Sajda Ashraf, Muhammad Taha, and Farman Ali Khan
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Molecular model ,Stereochemistry ,Bacillus ,Pyrimidinones ,Molecular Dynamics Simulation ,010402 general chemistry ,01 natural sciences ,Biochemistry ,chemistry.chemical_compound ,Structure-Activity Relationship ,Catalytic Domain ,Drug Discovery ,Structure–activity relationship ,Enzyme Inhibitors ,Molecular Biology ,Enzyme Assays ,chemistry.chemical_classification ,biology ,Molecular Structure ,010405 organic chemistry ,Aryl ,Organic Chemistry ,Active site ,Ligand (biochemistry) ,Urease ,In vitro ,0104 chemical sciences ,Molecular Docking Simulation ,Enzyme ,chemistry ,Thiourea ,biology.protein - Abstract
5-Acetyl-6-methyl-4-aryl-3,4-dihydropyrimidin-2(1H)-ones 1-43 were synthesized in a "one-pot" three component reaction and structurally characterized by various spectroscopic techniques such as 1H, 13C NMR, EI-MS, HREI-MS, and IR. All compounds were evaluated for their in vitro urease inhibitory activity. It is worth mentioning that except derivatives 1, 11, 12, and 14, all were found to be more potent than the standard thiourea (IC50 = 21.25 ± 0.15 µM) and showed their urease inhibitory potential in the range of IC50 = 3.70 ± 0.5-20.14 ± 0.1 µM. Structure-activity relationship (SAR) was rationalized by looking at the varying structural features of the molecules. However, molecular modeling study was performed to confirm the binding interactions of the molecules (ligand) with the active site of enzyme.
- Published
- 2017
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