Influence of residual chirality on the conformation and enzymatic degradation of glycopolypeptide based biomaterials

作     者：SHI Shun WANG JiaYu WANG TianRan REN Hui ZHOU YuHao LI Gao HE ChaoLiang CHEN XueSi SHI Shun;WANG JiaYu;WANG TianRan;REN Hui;ZHOU YuHao;LI Gao;HE ChaoLiang;CHEN XueSi

作者机构：CAS Key Laboratory of Polymer EcomaterialsChangchun Institute of Applied ChemistryChinese Academy of SciencesChangchun 130022China College of Applied Chemistry and EngineeringUniversity of Science and Technology of ChinaHefei 230026China Jilin Biomedical Polymers Engineering LaboratoryChangchun 130022China 

出 版 物：《Science China(Technological Sciences)》 (中国科学（技术科学英文版）)

年 卷 期：2021年第64卷第3期

页      面：641-650页

核心收录：

学科分类：0810[工学-信息与通信工程] 08[工学] 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）] 0702[理学-物理学] 0812[工学-计算机科学与技术（可授工学、理学学位）] 

基　　金：the National Natural Science Foundation of China(Grant Nos.51973218,51973220,21574127,51622307 and51833010) the Youth Innovation Promotion Association,CAS。 

主　　题：glycopolypeptides secondary structures enzymatic degradation chirality lectin binding 

摘      要：Glycopolypeptides as analogs of glycoproteins or glycosaminoglycans represent attractive building blocks for the construction of biomimetic biomaterials.However,the effects of amino acid chirality on the conformation and enzymatic degradation of glycopolypeptides are often overlooked.Here,we synthesized and characterized a range of glycopolypeptides composed of galactosylated poly(γ-propargylglutamate)s containing L-and/or D-glutamate residues.Glycopolypeptides containing pure Lglutamate residues were predominantlyα-helical,and the helicity increased over the degree of polymerization of the polypeptide backbones(24 to 44).The glycopolypeptide with pure D-glutamate residues adopted a mirroredα-helical conformation,whilst apparent random coil conformation was observed for the glycopolypeptide with equally mixed enantiomeric residues.The enzymatic degradation rates of the glycopolypeptides were markedly reduced following the introduction of D-glutamate residues into backbones.Galactoside pendants on these glycopolypeptides maintained their binding to peanut agglutinin.These structureproperty relationships provide new insight for the design of biomimetic biomaterials containing glycopolypeptides.