Homopolypeptide Vesicles Triggered by Side-Chain Hydration  

作　　者：Xin-Jie Shi Zhen Liu Yang-Chun Xie Min Xu Xiao-Hua He 

机构地区：[1]School of Chemistry and Molecular Engineering,East China Normal University,Shanghai 200241,China [2]School of Physics and Electronic Science,Shanghai Key Laboratory of Magnetic Resonance,East China Normal University,Shanghai 200241,China

出　　处：《Chinese Journal of Polymer Science》2022年第12期1631-1639,I0009,共10页高分子科学（英文版）

基　　金：financially supported by the National Natural Science Foundation of China (No.51773063);the Open Project of Shanghai Key Laboratory of Magnetic Resonance。

摘　　要：The formation of homopolypeptide vesicles and the identification of their self-assembly mechanism have been challenging issues in the field of polymer self-assembly. Using complementary circular dichroism(CD), Fourier transform infrared(FTIR) and low-field nuclear magnetic resonance(LF-NMR) spectroscopies, in this study we show that the higher hydrophilic ability of side-chains is a key factor for the formation of homopolypeptide vesicles from homo poly(Nε-carbobenzoxy-L-lysine)(PZlys), in which the vesicular structures are confirmed by scanning electron microscopy(SEM), transmission electron microscopy(TEM) and atomic force microscopy(AFM) measurements. Poly(γ-benzyl-Lglutamate-co-Nε-carbobenzoxy-L-lysine) [P(BLG-co-Zlys)] containing different molar ratios of BLG to Zlys units with the same peptide backbone as PZlys are used as the controls. The copolypeptides can only form micelles under the same conditions, due to the more hydrophobic nature of their side-chains. These results show that the specific side-chain structure of the polypeptides plays a fundamental role in the self-assembly of homopolypeptides. These findings can be useful to understand how the hydrophilicity of the side chains of amino acid residues on the surface of a protein affects its structures.

关 键 词：POLYPEPTIDE VESICLE Self-assembly HYDROPHOBIC MICELLE 

分 类 号：TQ311[化学工程—高聚物工业]