Exploring the binding site of the human muscarinic M3 receptor: Homology modeling and docking study

2007 ◽  
Vol 107 (8) ◽  
pp. 1794-1802 ◽  
Author(s):  
Liliana Ostopovici ◽  
Maria Mracec ◽  
Mircea Mracec ◽  
Ana Borota
Keyword(s):  
Homology Modeling ◽  
Binding Site ◽  
Docking Study ◽  
M3 Receptor

Homology modeling, binding site identification and docking study of human angiotensin II type I (Ang II-AT1) receptor

2015 ◽  
Vol 74 ◽  
pp. 42-48 ◽  
Author(s):  
Vivek K. Vyas ◽  
Manjunath Ghate ◽  
Kinjal Patel ◽  
Gulamnizami Qureshi ◽  
Surmil Shah
Keyword(s):  
Angiotensin Ii ◽  
Homology Modeling ◽  
Binding Site ◽  
Docking Study ◽  
At1 Receptor ◽  
Type I ◽  
Ang Ii ◽  
Binding Site Identification ◽  
Site Identification

A New Reactive Ketenaminal: Synthesis, Coupling Reaction, Tautomeric Study, Docking and Antimicrobial Evaluation of the Products

2020 ◽  
Vol 16 (6) ◽  
pp. 761-773
Author(s):  
Huda K. Mahmoud ◽  
Hanadi A. Katouah ◽  
Marwa F. Harras ◽  
Thoraya A. Farghaly
Keyword(s):  
Binding Site ◽  
Antimicrobial Agents ◽  
Coupling Reaction ◽  
Docking Study ◽  
Binding Mode ◽  
Binding Energies ◽  
Simple Method ◽  
Antimicrobial Evaluation ◽  
New Compounds ◽  
Active Methylene

Background: One of the most successful reagents used in the synthesis of the reactive enaminone is DMF-DMA, but it is very expensive with harmful effects on the human health and reacts with special compounds to generate the enaminone such as active methylene centers. Aim: In this article, we synthesized a new ketenaminal by simple method with inexpensive reagents (through desulfurization in diphenylether). Methods: Thus, a novel reactive ketenaminal (enaminone) was synthesized from the desulfurization of 2-((2-(4-chlorophenyl)-2-oxoethyl)thio)-5,7-bis(4-methoxyphenyl)pyrido[2,3-d]pyrimidin- 4(3H)-one with diphenylether. The starting keteneaminal was coupled with diazotized anilines via the known coupling conditions to give a new series of 2-(4-chlorophenyl)-1-(2-(arylhydrazono)-2- oxoethyl)-5,7-bis(4-methoxy-phenyl)pyrido[2,3-d]pyrimidin-4(1H)-ones. Results: The structures of the new compounds were elucidated based on their IR, 1H-NMR, 13CNMR, and Mass spectra. Moreover, the potency of these compounds as antimicrobial agents has been evaluated. The results showed that some of the products have high activity nearly equal to that of the used standard antibiotic. Additionally, the docking study was done to get the binding mode of the synthesized compounds with the binding site of the DHFR enzyme. The results of molecular docking of the synthesized arylhydrazono compounds are able to fit in DHFR binding site with binding energies ranging from -4.989 to -8.178 Kcal/mol. Conclusion: Our goal was achieved in this context by the synthesis of new ketenaminal from inexpensive reagents, which was utilized in the preparation of bioactive arylhydrazone derivatives.

Homology modeling in tandem with 3D-QSAR analyses: A computational approach to depict the agonist binding site of the human CB2 receptor

2011 ◽  
Vol 46 (9) ◽  
pp. 4489-4505 ◽  
Author(s):  
Elena Cichero ◽  
Alessia Ligresti ◽  
Marco Allarà ◽  
Vincenzo di Marzo ◽  
Zelda Lazzati ◽  
...  
Keyword(s):  
Homology Modeling ◽  
Binding Site ◽  
3D Qsar ◽  
Computational Approach ◽  
Agonist Binding ◽  
Cb2 Receptor

Cellulase enzyme: Homology modeling, binding site identification and molecular docking

2017 ◽  
Vol 1150 ◽  
pp. 61-67 ◽  
Author(s):  
K. Selvam ◽  
D. Senbagam ◽  
T. Selvankumar ◽  
C. Sudhakar ◽  
S. Kamala-Kannan ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Homology Modeling ◽  
Binding Site ◽  
Cellulase Enzyme ◽  
Binding Site Identification ◽  
Site Identification

scholarly journals In-silico Investigation of the Interaction between Beta-class Glutathione S-Transferase and Five Antibiotics, namely; Ampicillin, Tetracycline, Chloramphenicol, Ciprofloxacin and Cephalexin

2021 ◽  
Vol 25 (4) ◽  
pp. 497-502
Author(s):  
D. Shehu ◽  
S Danlami ◽  
M. Ya’u ◽  
A. Babandi ◽  
H.M. Yakasai ◽  
...  
Keyword(s):  
Amino Acids ◽  
Antibiotic Resistance ◽  
Molecular Docking ◽  
Binding Site ◽  
Substrate Binding ◽  
Docking Study ◽  
Glutathione S Transferase ◽  
Molecular Docking Study ◽  
Substrate Binding Site ◽  
Glutathione S Transferases

Glutathione s-transferases(GSTs) are enzymes involved in the conjugation and deactivation of various xenobiotics including drugs. Thisin-silico study was undertaken in order to investigate the interaction between beta-class glutathione s-transferase and five selected antibiotics, namely; ampicillin, tetracycline, chloramphenicol, ciprofloxacin and cephalexin using molecular docking study. RaptorX server was used to predict the amino acids involved at the binding sitewhile molecular docking study was employed in order to investigate the binding interactions.RaptorX predicted several amino acids which were different from the ones observed in molecular docking because of the variability in the substrate binding site of GSTs however, all the amino acids predicted by RaptorX were also found to be involved in the GSH binding.Lys107, Phe109, Ser110, Leu113, Trp114, His115 and Arg123, Leu168 were the amino acids involved in the binding of various antibiotics to the substrate binding site of the protein while Ala9, Cys10, Leu32, Tyr51, Val52, Pro53, Glu65 and Ala66were involved in the binding of the co-substrate GSH to the binding site of the protein. The results indicated that all the antibiotics showed a good binding affinity with the beta class GST and are therefore capable of deactivating the drugs. With these, finding a beta class GST inhibitors alongside antibiotics during a treatment of diseases will be of beneficial in the current fight against antibiotic resistance.

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