title: Characterizing the assembly behaviors of human amylin: a perspective derived from C-terminal variants.
abstract: The differences in the C-terminal domains of human amylin peptide variants initiate different aggregation processes and differences in the composition of the aggregates by affecting the hydrophobic cores, conformations, and intra-sheet interactions of the peptides, which have distinct effects on the cytotoxicity of the peptides.
authors.affiliation: Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing 100084, China.
authors.forename: Mei-Sha
authors.initials: MS
authors.lastname: Chen
authors.forename: De-Sheng
authors.initials: DS
authors.lastname: Zhao
authors.forename: Ye-Ping
authors.initials: YP
authors.lastname: Yu
authors.forename: Wei-Wei
authors.initials: WW
authors.lastname: Li
authors.forename: Yong-Xiang
authors.initials: YX
authors.lastname: Chen
authors.forename: Yu-Fen
authors.initials: YF
authors.lastname: Zhao
authors.forename: Yan-Mei
authors.initials: YM
authors.lastname: Li
mesh_terms: D000818:Animals; D000970:Antineoplastic Agents / Q000737:chemistry / Q000494:pharmacology*; D045744:Cell Line, Tumor; D002470:Cell Survival / Q000187:drug effects; D004305:Dose-Response Relationship, Drug; D004354:Drug Screening Assays, Antitumor; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D058228:Islet Amyloid Polypeptide / Q000737:chemistry / Q000494:pharmacology*; D011487:Protein Conformation; D051381:Rats; D013329:Structure-Activity Relationship
chemical_list: D000970:Antineoplastic Agents; D058228:Islet Amyloid Polypeptide