scholarly journals Molecular Docking and Kinetic Studies of the A226N Mutant of Deinococcus geothermalis Amylosucrase with Enhanced Transglucosylation Activity

2020 ◽  
Vol 30 (9) ◽  
pp. 1436-1442
Author(s):  
Seungpyo Hong ◽  
Inonge Noni Siziya ◽  
Myung-Ji Seo ◽  
Cheon-Seok Park ◽  
Dong-Ho Seo
Keyword(s):  
Molecular Docking ◽  
Kinetic Studies ◽  
Deinococcus Geothermalis

scholarly journals Molecular Docking and Reaction Kinetic Studies of Chrysin Binding to Serum Albumin

2014 ◽  
Vol 9 (2) ◽  
pp. 1934578X1400900 ◽  
Author(s):  
Bingli Jiang ◽  
Anran Zhao ◽  
Jianhua Miao ◽  
Pengfei Chang ◽  
Hailin Chen ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Serum Albumin ◽  
Reaction Kinetic ◽  
Reaction Order ◽  
Kinetic Studies ◽  
Cd Spectroscopy ◽  
Reaction Enthalpy ◽  
Binding Properties ◽  
Hydrophobic Force ◽  
Physiological Conditions

The binding properties of chrysin with serum albumin (SA) were investigated under physiological conditions by calorimetry, circular dichroism (CD) spectroscopy, and molecular modeling. Based on the thermodynamic data, molar reaction enthalpy, reaction order ( n) and the rate constant ( k) were calculated. The results of CD spectroscopy showed that chrysin could bind to SA and the conformation of SA did not have any high-ordered structural change. Computational mapping revealed chrysin binding to the subdomain IB in SA. The chrysin-serum albumin complex was stabilized by hydrophobic force and hydrogen bonding and the reaction was a spontaneous process.

Computational Analysis and Synthesis of Syringic Acid Derivatives as Xanthine Oxidase Inhibitors

2020 ◽  
Vol 16 (5) ◽  
pp. 643-653 ◽  
Author(s):  
Neelam Malik ◽  
Anurag Khatkar ◽  
Priyanka Dhiman
Keyword(s):  
Antioxidant Activity ◽  
Uric Acid ◽  
Molecular Docking ◽  
Xanthine Oxidase ◽  
Kinetic Studies ◽  
Inhibitory Effect ◽  
Syringic Acid ◽  
Antioxidant Potential ◽  
Xanthine Oxidase Inhibitors ◽  
Analysis And Synthesis

Background: Xanthine oxidase (XO; EC 1.17.3.2) has been considered as a potent drug target for the cure and management of pathological conditions prevailing due to high levels of uric acid in the bloodstream. The role of xanthine oxidase has been well established in the generation of hyperuricemia and gout due to its important role in catalytic oxidative hydroxylation of hypoxanthine to xanthine and further catalyses of xanthine to generate uric acid. In this research, syringic acid, a bioactive phenolic acid was explored to determine the capability of itself and its derivatives to inhibit xanthine oxidase. Objective: The study aimed to develop new xanthine oxidase inhibitors from natural constituents along with the antioxidant potential. Methods: In this report, we designed and synthesized syringic acid derivatives hybridized with alcohol and amines to form ester and amide linkage with the help of molecular docking. The synthesized compounds were evaluated for their antioxidant and xanthine oxidase inhibitory potential. Results: Results of the study revealed that SY3 produces very good xanthine oxidase inhibitory activity. All the compounds showed very good antioxidant activity. The enzyme kinetic studies performed on syringic acid derivatives showed a potential inhibitory effect on XO ability in a competitive manner with IC50 value ranging from 07.18μM-15.60μM and SY3 was revealed as the most active derivative. Molecular simulation revealed that new syringic acid derivatives interacted with the amino acid residues SER1080, PHE798, GLN1194, ARG912, GLN 767, ALA1078 and MET1038 positioned inside the binding site of XO. Results of antioxidant activity revealed that all the derivatives showed very good antioxidant potential. Conclusion: Molecular docking proved to be an effective and selective tool in the design of new syringic acid derivatives .This hybridization of two natural constituents could lead to desirable xanthine oxidase inhibitors with improved activity.

Enzyme Inhibition, Kinetic, and Molecular Docking Studies of α-glucosidase

2020 ◽  
Vol 16 (2) ◽  
pp. 155-161
Author(s):  
Ebrahim S. Moghadam ◽  
Mohammad A. Faramarzi ◽  
Somayeh Imanparast ◽  
Mohsen Amini
Keyword(s):  
Molecular Docking ◽  
Active Site ◽  
Competitive Inhibition ◽  
Kinetic Studies ◽  
Developed Countries ◽  
Docking Studies ◽  
Antidiabetic Activity ◽  
Active Site Residues ◽  
Efficient Treatment ◽  
Enzyme Active Site

Background: Diabetes mellitus (DM) is an important global health problem especially in developed countries and insufficient lifestyle induces this phenomenon. Finding efficient treatment for DM is an interesting goal for researchers. Objective: Herein we tried to design and synthesize a series of quinazoline derivatives and investigate their bioactivity as possible α-Glucosidase inhibitor agents. Method: Compounds 1-14 were synthesized using a multicomponent reaction. 1HNMR, 13C NMR, MS, and IR spectroscopy were used for the characterization of synthesized compounds. α- Glucosidase inhibitory activity of compounds 1-14 was evaluated using p-nitrophenyl‐α‐Dglucopyranoside (pNPG) as a substrate of the α-glucosidase enzyme (EC3.2.1.20, Saccharomyces cerevisiae). The mechanism of inhibition of the α-glucosidase enzyme was investigated using kinetic studies. Molecular docking was also done using autodock software to find the possible mode of interaction of compound 8 and the enzyme active site. Results: Most of the tested compounds showed higher activity in inhibition of the enzyme in comparison to the standard, acarbose. Compound 8 exerted the best activity with the IC50 value of 291.5 μM. A kinetic study indicated a competitive inhibition of the α-glucosidase enzyme by compound 8. Finally, docking studies showed the interactions between compound 8 and enzyme active site residues. Conclusion: 2,4-Diarylquinazoline scaffold has good antidiabetic activity, so it is interesting to synthesize more 2,4-diarylquinazoline derivatives and evaluate their antidiabetic activities.

scholarly journals A new guanylhydrazone derivative as a potential acetylcholinesterase inhibitor for Alzheimer's disease: synthesis, molecular docking, biological evaluation and kinetic studies by nuclear magnetic resonance

RSC Advances ◽  
2017 ◽  
Vol 7 (54) ◽  
pp. 33944-33952 ◽  
Author(s):  
Denise Cristian Ferreira Neto ◽  
Marcelle de Souza Ferreira ◽  
Elaine da Conceição Petronilho ◽  
Josélia Alencar Lima ◽  
Sirlene Oliveira Francisco de Azeredo ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Nuclear Magnetic Resonance ◽  
Molecular Docking ◽  
Magnetic Resonance ◽  
In Silico ◽  
Acetylcholinesterase Inhibitor ◽  
Kinetic Studies ◽  
Biological Evaluation ◽  
Nuclear Magnetic

Molecular docking, in silico studies and NMR show that the new guanylhydrazone is a promising compound for the treatment of Alzheimer's disease.

Computational and Kinetic Studies of Acetylcholine Esterase Inhibition by Phenserine

2019 ◽  
Vol 25 (18) ◽  
pp. 2108-2112 ◽  
Author(s):  
Shams Tabrez ◽  
Ghazi A. Damanhouri
Keyword(s):  
Molecular Docking ◽  
Mixed Type ◽  
Kinetic Studies ◽  
Docking Study ◽  
Docking Studies ◽  
Catalytic Site ◽  
Dependent Manner ◽  
Molecular Docking Study ◽  
Ic50 Value ◽  
Current Article

Background: The inhibition of cholinesterase enzymes is one of the promising strategies to manage several neurological disorders that include Alzheimer's disease (AD). Material and Methods: In the current article, we estimated the potential inhibition of acetyl cholinesterase (AChE) by phenserine using slightly modified Ellman assay. To find out the binding interactions of phenserine with the catalytic site of AChE, a molecular docking study was also performed. Results: Phenserine was found to inhibit Electrophorus electricus AChE in a dose-dependent manner with an IC50 value of 0.013 µM. The kinetic analyses indicate that phenserine inhibits AChE in a mixed type manner (competitive and uncompetitive) with Ki values of 0.39 μmole/l and 0.21 µmole/l, respectively. On the other hand, Km and Vmax values were found to be 0.17 µM and 0.39 µM, respectively. The molecular docking studies indicate efficient binding of phenserine through 6 hydrogen bonds, 4 pi-alkyl interactions, and 1 pi-pi interaction within the AChE catalytic pocket. Conclusion: Results of our computational and kinetics studies indicated a mixed type inhibition by phenserine at AChE catalytic site.

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

2020 ◽  
Vol 28 (11) ◽  
pp. 115467 ◽  
Author(s):  
Emmanuel Oloruntoba Yeye ◽  
Kanwal ◽  
Khalid. Mohammed Khan ◽  
Sridevi Chigurupati ◽  
Abdul Wadood ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Kinetic Studies ◽  
Triazole Derivatives ◽  
Inhibitory Activities

Phosphonic and Phosphinic Acid Derivatives as Novel Tyrosinase Inhibitors: Kinetic Studies and Molecular Docking

2019 ◽  
Vol 16 (7) ◽  
Author(s):  
Ewa Wolińska ◽  
Katarzyna Hałdys ◽  
Jerzy Góra ◽  
Tomasz K. Olszewski ◽  
Bogdan Boduszek ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Phosphinic Acid ◽  
Kinetic Studies ◽  
Tyrosinase Inhibitors
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