Binding Affinity of Labeling Molecules on Two Conformations of hIAPP20-29

• 作 者: Yue Yu Chenxuan Wang Yanlian Yang Chen Wang
• 机 构: NationalCenterforNanoscienceandTechnology,No.11ZhongGuanCunBeiYiTiao,100190Beijing,P.R.China
• 出 处: 第十三届中国国际多肽大会
• 发表日期: 2014年6期
• 关键词: Amylin IAPP Amyloid Parallel Anti parallel Binding affinity Scanning tunneling m

　　Human islet amyloid polypeptide(hIAPP)is strongly relevant to the development of type 2 diabetes [1].The sequence of hIAPP20-29 has been proved to be the core of hIAPP fibrillation.Previous studies on exploring its structure concluded differently on either parallel or anti parallel structures.Which is the dominant structure? How to distinguish between them? Labeling molecules such as Thioflavin-T are widely used to visualize and quantify the presence of amyloid based on their binding to beta sheet-rich structures.Whether they have any preference on parallel or anti parallel structures is still uncertain.