Influence of residual chirality on the conformation and enzymatic degradation of glycopolypeptide based biomaterials
Influence of residual chirality on the conformation and enzymatic degradation of glycopolypeptide based biomaterials
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DOI：
10.1007/s11431-020-1713-2
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发表时间：
2021-01
期刊：
影响因子：
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通讯作者：
Shun Shi;Jiayu Wang;Tianran Wang;Hui Ren;Yuhao Zhou;Gao Li;Chaoliang He;Xuesi Chen
中科院分区：
文献类型：
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作者：
Shun Shi;Jiayu Wang;Tianran Wang;Hui Ren;Yuhao Zhou;Gao Li;Chaoliang He;Xuesi Chen
糖多肽作为糖蛋白或糖胺聚糖的类似物，是构建仿生生物材料的诱人构件。然而，氨基酸的手性对糖多肽的构象和酶降解的影响往往被忽视。在这里，我们合成并表征了一系列由含γ-和/或D-谷氨酸残基的半乳糖化的聚(-丙交酯谷氨酸)S组成的糖多肽。含有纯L-谷氨酸残基的糖多肽以α-螺旋为主，螺旋度随多肽骨架聚合度的增加而增加(24~44)。含有纯D-谷氨酸残基的糖多肽采用镜像α-螺旋构象，而含有均匀混合对映体残基的糖多肽则呈明显的无规卷曲构象。在骨骼中引入D-谷氨酸残基后，糖多肽的酶降解速率明显降低。这些糖多肽上的半乳糖苷挂件与花生凝集素保持结合。这些结构与性质的关系为含糖多肽的仿生生物材料的设计提供了新的思路。
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 L-glutamate residues were predominantly α-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 mirrored α-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 structure-property relationships provide new insight for the design of biomimetic biomaterials containing glycopolypeptides.