title: Rational design of an orthosteric regulator of hIAPP aggregation.
abstract: Developing compounds regulating amyloid toxic oligomer but not fibril formation should constitute an effective strategy for the treatment of diabetes. Based on the full understanding of the folding mechanism, we designed an orthosteric helix regulator that can promote hIAPP to assemble into large non-cytotoxic oligomers. As a result, the islet cells were protected.
authors.affiliation: Department of Chemistry, Key Laboratory of Bioorganic Phosphorus Chemistry & Chemical Biology (Ministry of Education), Tsinghua University, Beijing 10084, P. R. China. liym@mail.tsinghua.edu.cn.
authors.forename: De-Sheng
authors.initials: DS
authors.lastname: Zhao
authors.forename: Yong-Xiang
authors.initials: YX
authors.lastname: Chen
authors.forename: Yan-Mei
authors.initials: YM
authors.lastname: Li
mesh_terms: D000494:Allosteric Regulation / Q000187:drug effects; D000818:Animals; D045744:Cell Line, Tumor; D015195:Drug Design; D006801:Humans; D058228:Islet Amyloid Polypeptide / Q000737:chemistry*; D008958:Models, Molecular; D010455:Peptides / Q000494:pharmacology*; D055503:Protein Multimerization / Q000187:drug effects*; D017433:Protein Structure, Secondary / Q000187:drug effects; D051381:Rats
chemical_list: D058228:Islet Amyloid Polypeptide; D010455:Peptides