title: Effect of the surface chemistry of insulin fibrils on the aggregation rate.
abstract: Structure transition cascade: Insulin fibrils undergo a secondary structural transition-from the α-rich to the β-rich form-upon progressively increasing the incubation time from 0.5 to ten hours. Atomic force microscopy measurements show that the fibril surface chemistry changes from hydrophilic to hydrophobic and the aggregation rate increases fivefold.
authors.affiliation: Department of Chemistry, National Sun Yat-sen University, 70 Lien-hai Rd., Kaohsiung, Taiwan 80424 (Republic of China); School of Pharmacy, College of Pharmacy, Kaohsiung Medical University, 100 Shih-Chuan 1st Road, Kaohsiung, Taiwan 80708 (Republic of China). shsieh@facmail.nsysu.edu.tw.
authors.forename: Shuchen
authors.initials: S
authors.lastname: Hsieh
authors.forename: Chiung-Wen
authors.initials: CW
authors.lastname: Hsieh
authors.forename: Hsuan-Hung
authors.initials: HH
authors.lastname: Chou
authors.forename: Chiung-Wen
authors.initials: CW
authors.lastname: Chang
authors.forename: Ling-Ya
authors.initials: LY
authors.lastname: Chu
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D007328:Insulin / Q000737:chemistry*; D018625:Microscopy, Atomic Force / Q000379:methods; D017433:Protein Structure, Secondary
chemical_list: D000682:Amyloid; D007328:Insulin
keywords: adhesion force; atomic force microscopy; fibrous proteins; hydrophobic effect; protein engineering