一种新型多肽仿生材料的自组装结构研究  

Study on the self-assembly structure of a novel peptide biomimetic material

作　　者：周庆翰[1] 罗建斌[1] 林娟[2] 廖戎[1] 万静[1] 马晨[1] 

机构地区：[1]西南民族大学化学与环境保护工程学院,四川成都610041 [2]成都医学院生物医学系,四川成都610083

出　　处：《西南民族大学学报（自然科学版）》2011年第4期632-634,共3页Journal of Southwest Minzu University(Natural Science Edition)

基　　金：西南民族大学学生创新项目资助

摘　　要：利用天然蛋白质氨基酸序列设计生物仿生材料是近年来兴起的一个热门研究领域.本文中将蚕丝蛋白特征氨基酸序列(Gly-Ala-Gly-Ala-Gly-Ser)部分引入离子互补型多肽RADA16-I:(Arg-Ala-Asp-Ala)4中,设计了新型多肽RAGA16:Arg-Ala-Asp-Ala-Gly-Ala-Gly-Ala-Arg-Ala-Asp-Ala-Gly-Ala-Gly-Ser.采用原子力显微镜(AFM)等技术对多肽的自组装结构进行了研究,发现新型多肽自组装形成数微米长的纤维结构,通过分析得知多肽二级结构中Silk I结构成分比例增加是导致其纳米结构的变化主要原因.因此推测蚕丝蛋白特征序列对改变材料纳米结构有明显作用.Designing bio-mimetic materials by mimicing the amino acid sequence of natural proteins has received considerable attention in recent years. A novel self-assembly peptide, Arg-Ala-Asp-Ala-Gly-Ala-Gly-Ala-Arg-Ala-Asp-Ala-Gly-Ala-Gly-Ser is designed by partially inserting the characteristic silk fibroin motif Gly-Ala-Gly-Ala-Gly-Ser into an ionic self-complementary peptide RADA16-I, （Arg-Ala-Asp-Ala）4. Modem analysis methods are utilized to study the self-assembly structure such as atomic force microscopy （AFM）. The novel peptides formed fibers at several microns due to the increase of the silk I structure form fibroin motif segment, indicating the critical role of the characteristic silk fibroin motif in changing the structure of nano-matierials.

关 键 词：蚕丝蛋白 自组装多肽 纳米结构 

分 类 号：R318.08[医药卫生—生物医学工程]