"In silico docking analysis of selected phytochemicals with dipeptidyl " by Christensen P. Calibo, Jewel Denisse T. Fontanilla et al.

Date of Completion

7-2021

Document Type

Thesis

Degree Name

Bachelor of Science in Biochemistry

Keywords

Computer Simulation, Phytochemicals

Abstract

Dipeptidyl peptidase (DPP)-IV is a cell-surface aminopeptidase that is responsible for the half-life of GIP and GLP-1 which affect blood glucose levels. Inhibition of DPP-IV may prolong the life of the said proteins resulting in a decrease in blood glucose. Secondary metabolites exhibit biological processes that may inhibit diseases such as Type 2 Diabetes Mellitus – a condition characterized by abnormally high blood glucose levels. Thirty phytochemicals including alkaloids, flavonoids, phenolics, and terpenoids were docked against DPP-IV to examine its inhibitory properties. DPP-IV-ligand complex docking was carried out using AutoDock Vina program in UCSF Chimera Software. Binding affinity, number of amino acid interactions, and bond distance were utilized to determine potential DPP-IV inhibitors. Results revealed that tiliroside had the highest binding affinity among the 30 phytochemicals, andrographolide reported the highest number of interactions in the active site of DPP-IV, and kaempferol exhibited the shortest bond distance.

First Advisor

Tabitha L. Amora

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