Docking simulation of Chemerin-9 and ChemR23 receptor

EasyChair Preprint 1552

Abstract

Chemerin-9 is a nonapeptide that corresponds to the YFPGQFAFS sequence on the C-terminal side of Chemerin protein. In recent years, in clinical studies and animal studies using mice, it has been reported that Chemerin-9 binds to the ChemR23 receptor and can suppress the inflammation-related diseases such as arteriosclerosis. In this study, molecular dynamics simulations were performed with the Chemerin-9 peptide to identify structures with high and low free energy. Docking simulations of these structures of Chemerin-9 and ChemR23 receptor were performed, and the docking model with the lowest free energy and binding energy of Chemerin was identified. For this model, the evaluation of binding sites and binding forces is performed. Based on these findings, we will aim to give insights to the development of new drugs that suppress arteriosclerosis.

Keyphrases: Atherosclerosis, ChemR23, Chemerin-9, docking simulations, hydrogen bonds, ligand, molecular dynamics simulations, receptor

@booklet{EasyChair:1552,
  author    = {Keiichi Nobuoka and Hironao Yamada and Takeshi Miyakawa and Ryota Morikawa and Takuya Watanabe and Masako Takasu},
  title     = {Docking simulation of Chemerin-9 and ChemR23 receptor},
  howpublished = {EasyChair Preprint 1552},
  year      = {EasyChair, 2019}}