Responses of Transmembrane Peptide and Lipid Chains to Hydrophobic Mismatch  

作　　者：YANG Lei LI Jian-tao QI Hai-yan LI Fei 

机构地区：[1]State Key Laboratory of Supramolecular Structure and Materials,Jilin University,Changchun 130012,P.R.China

出　　处：《Chemical Research in Chinese Universities》2012年第4期732-736,共5页高等学校化学研究（英文版）

基　　金：Supported by the National Natural Science Foundation of China(Nos.20973083,20934002)

摘　　要：Hydrophobic mismatch between the hydrophobic length of membrane proteins and hydrophobic thickness of membranes is a crucial factor in controlling protein function and assembly.We combined fluorescence with circular dichroism（CD） and attenuated total reflection infrared（ATR-IR） spectroscopic methods to investigate the behaviors of the peptide and lipids under hydrophobic mismatch using a model peptide from the fourth transmembrane domain of natural resistance-associated macrophage protein 1（Nramp1）,the phosphatidylcholines（PCs） and phosphatidylglycerols（PGs） with different lengths of acyl chains（14：0,16：0 and 18：0）.In all PG lipid membranes,the peptide forms stable α-helix structure,and the helix axis is parallel to lipid chains.The helical span and orientation hardly change in varying thickness of PG membranes,while the lipid chains can deform to accommodate to the hydrophobic surface of embedded peptide.By comparison,the helical structures of the model peptide in PC lipid membranes are less stable.Upon incorporation with PC lipid membranes,the peptide can deform itself to accommodate to the hydrophobic thickness of lipid membranes in response to hydrophobic mismatch.In addition,hydrophobic mismatch can increase the aggregation propensity of the peptide in both PC and PG lipid membranes and the peptide in PC membranes has more aggregation tendency than that in PG membranes.Hydrophobic mismatch between the hydrophobic length of membrane proteins and hydrophobic thickness of membranes is a crucial factor in controlling protein function and assembly.We combined fluorescence with circular dichroism（CD） and attenuated total reflection infrared（ATR-IR） spectroscopic methods to investigate the behaviors of the peptide and lipids under hydrophobic mismatch using a model peptide from the fourth transmembrane domain of natural resistance-associated macrophage protein 1（Nramp1）,the phosphatidylcholines（PCs） and phosphatidylglycerols（PGs） with different lengths of acyl chains（14：0,16：0 and 18：0）.In all PG lipid membranes,the peptide forms stable α-helix structure,and the helix axis is parallel to lipid chains.The helical span and orientation hardly change in varying thickness of PG membranes,while the lipid chains can deform to accommodate to the hydrophobic surface of embedded peptide.By comparison,the helical structures of the model peptide in PC lipid membranes are less stable.Upon incorporation with PC lipid membranes,the peptide can deform itself to accommodate to the hydrophobic thickness of lipid membranes in response to hydrophobic mismatch.In addition,hydrophobic mismatch can increase the aggregation propensity of the peptide in both PC and PG lipid membranes and the peptide in PC membranes has more aggregation tendency than that in PG membranes.

关 键 词：Hydrophobic mismatch Transmembrane peptide Fluorescence Circular dichroism（CD） Attenuated total reflection infrared（ATR-IR） 

分 类 号：Q516[生物学—生物化学] TP212[自动化与计算机技术—检测技术与自动化装置]