title: Co-assembly of human islet amyloid polypeptide (hIAPP)/insulin.
abstract: The pathogenesis of type II diabetes can be linked to cosecreted hIAPP/insulin interacting with cell membranes. Here we investigate the nanostructures by co-assembling hIAPP and insulin on surfaces. By tuning the hIAPP/insulin ratio, atomic force microscopy reveals the resulting nanostructure morphology changes from fibrils to oligomers, to annular. Implications for in vivo studies are discussed.
authors: Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing, 100084, China.
authors: Peng
authors: P
authors: Liu
authors: Shuai
authors: S
authors: Zhang
authors: Mei-sha
authors: MS
authors: Chen
authors: Qian
authors: Q
authors: Liu
authors: Chenxuan
authors: C
authors: Wang
authors: Chen
authors: C
authors: Wang
authors: Yan-Mei
authors: YM
authors: Li
authors: Flemming
authors: F
authors: Besenbacher
authors: Mingdong
authors: M
authors: Dong
mesh_terms: D000682:Amyloid / Q000378:metabolism / Q000648:ultrastructure*; D003924:Diabetes Mellitus, Type 2 / Q000378:metabolism* / Q000473:pathology; D006801:Humans; D007328:Insulin / Q000378:metabolism*; D058228:Islet Amyloid Polypeptide / Q000378:metabolism*; D018625:Microscopy, Atomic Force
chemical_list: D000682:Amyloid; D007328:Insulin; D058228:Islet Amyloid Polypeptide