Interactions of human islet amyloid polypeptide with lipid structure of different curvatures  

作　　者：Le Mei Wenhui Shen Xuwei Wu Jie Liu Dechang Li Baohua Ji 

机构地区：[1]Biomechanics and Biomaterials Laboratory,Department of Applied Mechanics,Beijing Institute of Technology,Beijing 100081,China [2]Institute of Applied Mechanics,Department of Engineering Mechanics,Zhejiang University,Hangzhou 310027,China

出　　处：《Theoretical & Applied Mechanics Letters》2020年第6期412-418,共7页力学快报（英文版）

基　　金：supported by funds from the National Natural Science Foundation of China(Grants 11932017,11772054,11772055,and 11532009);supported by the Fundamental Research Funds for the Central Universities(Grant 2019QNA4060)。

摘　　要：Curvature is one of the most important features of lipid membranes in living cells,which significantly influences the structure of lipid membranes and their interaction with proteins.Taken the human islet amyloid polypeptide(h IAPP),an important protein related to the pathogenesis of type II diabetes,as an example,we performed molecular dynamics(MD)simulations to study the interaction between the protein and the lipid structures with varied curvatures.We found that the lipids in the high curvature membrane pack loosely with high mobility.The h IAPP initially forms H-bonds with the membrane surface that anchored the protein,and then inserts into the membrane through the hydrophobic interactions between the residues and the hydrophobic tails of the lipids.h IAPP can insert into the membrane more deeply with a larger curvature and with a stronger binding strength.Our result provided important insights into the mechanism of the membrane curvature-dependent property of proteins with molecular details.

关 键 词：Lipid membrane CURVATURE Human islet amyloid polypeptide Molecular dynamics 

分 类 号：Q51[生物学—生物化学]