Open AccessANTICHOLINESTERASE ACTIVITY OF OCTA PEPTIDES RELATED TO HUMAN HISTATIN 8: IN-SILICO DRUG DESIGN AND IN-VITRO
Author(s) -
Pandurangan Perumal,
Vasudevan Mani,
Sridevi Chigurupati,
Manikandan Selvaraj
Publication year - 2017
Publication title -
asian journal of pharmaceutical and clinical research
Language(s) - English
Resource type - Journals
eISSN - 2455-3891
pISSN - 0974-2441
DOI - 10.22159/ajpcr.2017.v10i6.17697
Subject(s) - in silico , acetylcholinesterase , aché , ic50 , in vitro , docking (animal) , acetylcholinesterase inhibitor , chemistry , pharmacology , enzyme , biochemistry , peptide , donepezil , biology , medicine , veterinary medicine , dementia , disease , gene
Objective: To evaluate the octapeptides related to human histatin 8 by in-silico and in-vitro studies.Method: Schrodinger, LLC and Ellman’s method.Results: The compound HH1 and HH2 was found to be potent docking score of −9.494 and −7.401 against acetylcholinesterase (AChE) enzyme. The IC50 value of HH1 and HH2 was found to be 0.39±0.28 and 0.78±0.15 μg/mL. However, these compounds are shown to be highly effective as compared with the control AChE inhibitor donepezil (0.065±0.0050 μg/mL).Conclusion: In-silico docking study was conducted for the designed octapeptides related to human histatin 8 against AChE enzyme shows significance binding affinity toward HH1 and HH2 peptides and the AChE inhibitory activity of octapeptides shown to be a highly potent inhibitor as compared with control donepezil.