文献类型：期刊文献

英文题名：Ordering of polypeptides in liquid crystals, gels and micelles

作者：Cai, Chunhua[1]; Lin, Jiaping[1]; Zhuang, Zeliang[1]; Zhu, Wenjie[1]

机构：[1] Key Laboratory for Ultrafine Materials of Ministry of Education, School of Materials Science and Engineering, East China University of Science and Technology, Shanghai 200237, China

年份：2013

卷号：259

起止页码：159

外文期刊名：Advances in Polymer Science

收录：EI(收录号：20242616496405)

语种：英文

外文关键词：Chains - Conformations - Crystal structure - Liquid crystals - Micelles - Polypeptides - Proteins - Self assembly

摘要：Ordered structures assembled from polypeptides have attracted a great deal of attention over the past few decades. Both α-helix and β-sheet conformations of polypeptides support the formation of ordered structures during the assembly process. For polypeptides with α-helix conformation, the ordered structures are formed mainly by side-by-side packing of α-helix rods. For polypeptides with β-sheet conformation, ordering of the chains can be achieved by parallel or antiparallel packing. The ordering characteristic of polypeptide chains gives rise to fascinating assembly behaviors of polypeptide homopolymers and copolymers in solution. Usually, a decrease in polymer concentration is accompanied by the assembly of polypeptides into liquid crystals (LCs), gels, and micelles. This review describes the ordering structures of polypeptides in these assemblies. In LC structures, polypeptide homopolymer chains are packed in a highly ordered fashion with smectic, nematic, and cholesteric phases. Both polypeptide homopolymers and copolymers support the formation of gels in solution. The dislocated side-by-side packing of polypeptide helices is the basic ordering characteristic of the polypeptides in gels. Compared with the α-helix conformation, gels formed from polypeptides with β-sheet conformation show higher stability. In dilute solutions, amphiphilic polypeptide copolymers can self-assemble into micelles that include cylinders, vesicles, and complex hierarchical structures. The ordering nature of the polypeptide chains can be observed in the assemblies. The close relationship with proteins makes polypeptides and their assembly structures ideal models for protein research and promising candidates in biorelated applications. ? Springer-Verlag Berlin Heidelberg 2013.