Modelling P1-M binding to enzymes of the chitin degradation pathway in asian corn borer, Ostrinia furnacalis (Guenne)

Issue Date

4-2016

Abstract

Discovery and development of new mode of action chemical entities is important for increasing the number of effective tools for management of insect resistance to insecticides. inverse in silicomolecular docking was utilized to identify possible enzyme targets of P1-M in O. furnacalis. Tight binding interaction of P1-M was observed in chitinase (-8.6 kcal/mol) and ß-N-Acetyl-D-hexosaminidase (-8.1 kcal/mol), respectively. Hydrogen bonding and hydrophobic interactions contributed by the amphiphilic property of P1-M resulted in tight binding in the active site of the target enzymes. Molecular interaction of P1-M with O.furnacalis chitin synthase could not be properly evaluated because of the lack of accurate model of its 3D structure. Taken together, the structure-based in silico docking study revealed that P1-M is a possible strong inhibitor of enzymes responsible for chitin degradation pathway in O. furnacalis.

Source or Periodical Title

The Philippine Entomologist

ISSN

0048-3753

Volume

30

Issue

1

Page

53-62

Document Type

Article

Frequency

semi-annually

Physical Description

illustrations ; tables

Language

English

En – AGROVOC descriptors

OSTRINIA FURNACALIS; INSECTA; PESTS OF PLANT; CHITIN; MODE OF ACTION; PESTICIDAL PROPERTIES

This document is currently not available here.

Share

COinS