title: Light-driven porphyrin modulating fibrillation of hIAPP(20-29) peptide.
abstract: The human Islet amyloid polypeptide (20-29) (hIAPP20-29) is considered to be the core fibrillating fragment of hIAPP, which is associated with the pathogenesis of Type-II diabetes mellitus. A current challenge is the discovery of an efficient way to modulate amyloid aggregation and inhibit the toxicity of its aggregates. In this work, photoexcited porphyrins are successfully used to inhibit the fibrillation of hIAPP20-29. Insights on the inhibitory mechanism are explored by the analysis of the secondary structure, the morphology and the mechanical properties of amyloid aggregates. In addition, photoexcited porphyrins displayed a retained inhibitory effect on hIAPP20-29aggregation without irradiation. These findings may establish a new avenue to inhibit the aggregation of amyloid peptide hIAPP and enrich the current selection of modulators.
authors.affiliation: Institute for Advanced Materials, Jiangsu University, Zhenjiang 212013, China.
authors.forename: Guodong
authors.initials: G
authors.lastname: Yang
authors.affiliation: Institute for Advanced Materials, Jiangsu University, Zhenjiang 212013, China. Electronic address: liul@ujs.edu.cn.
authors.forename: Lei
authors.initials: L
authors.lastname: Liu
authors.affiliation: Institute for Advanced Materials, Jiangsu University, Zhenjiang 212013, China; Interdisciplinary Nanoscience Center (iNANO), Aarhus University, DK-8000 Aarhus C, Denmark.
authors.forename: Jie
authors.initials: J
authors.lastname: Wang
authors.affiliation: Interdisciplinary Nanoscience Center (iNANO), Aarhus University, DK-8000 Aarhus C, Denmark.
authors.forename: Christian
authors.initials: C
authors.lastname: Bortolini
authors.affiliation: Interdisciplinary Nanoscience Center (iNANO), Aarhus University, DK-8000 Aarhus C, Denmark. Electronic address: dong@inano.au.dk.
authors.forename: Mingdong
authors.initials: M
authors.lastname: Dong
mesh_terms: D000682:Amyloid / Q000737:chemistry* / Q000528:radiation effects; D006801:Humans; D058228:Islet Amyloid Polypeptide; D008027:Light; D055595:Mechanical Phenomena; D018625:Microscopy, Atomic Force; D010446:Peptide Fragments / Q000737:chemistry* / Q000528:radiation effects; D011166:Porphyrins / Q000737:chemistry* / Q000528:radiation effects; D017433:Protein Structure, Secondary
chemical_list: D000682:Amyloid; C521761:IAPP(20-29) peptide; D058228:Islet Amyloid Polypeptide; D010446:Peptide Fragments; D011166:Porphyrins
keywords: Amyloid fibril; Amyloid peptide aggregation; Nanomechanical mapping; Scanning probe microscopy