Stability and orientation of cecropin P1 on maleimide self-assembled monolayer(SAM) surfaces and suggested functional mutations

作     者：Shuai Wei Charles L.Brooks Ⅲ 

作者机构：Department of ChemistryUniversity of Michigan Department of BiophysicsUniversity of Michigan 

出 版 物：《Chinese Chemical Letters》 (中国化学快报（英文版）)

年 卷 期：2015年第26卷第4期

页      面：485-490页

核心收录：

学科分类：081704[工学-应用化学] 07[理学] 080202[工学-机械电子工程] 08[工学] 0817[工学-化学工程与技术] 070305[理学-高分子化学与物理] 080501[工学-材料物理与化学] 0805[工学-材料科学与工程（可授工学、理学学位）] 0703[理学-化学] 0802[工学-机械工程] 

主　　题：Coarse grained simulationKB Go like modelPeptide surface interactionThermal stabilityOrientationMutation 

摘      要：One of the main challenges of biosensor design is to understand the protein or peptide stability on the chip in high resolution structural detail. Since conventional experimental methods are limited by the resolution for their applications on surface tethered peptides/proteins, a recently developed coarse grained simulation method is employed to explore the peptide/surface interaction in residue-level resolution. This work shows how the coarse grained model successfully describes peptide-surface interactions by evaluating thermal stability of the peptide cecropin PI in bulk solution and on surfaces by physical adsorption and chemical tethering. The simulation also reproduces observations of peptide orientations on the self-assembled monolayer surface from earlier experimental work. Additionally, using knowledge obtained from the simulations, specific mutations are suggested and the desired structure and pose on the surface is obtained. In summary, this work sheds a light on the reasonable biosensor design that is ~uided by simulations.