Light-driven porphyrin modulating fibrillation of hIAPP(20-29) peptide

Guodong Yang, Lei Liu*, Jie Wang, Christian Bortolini, Mingdong Dong

*Corresponding author for this work

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Abstract

The human Islet amyloid polypeptide (20-29) (hIAPP(20-29)) 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 hIAPP(20-29). 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 hIAPP(20-29) aggregation without irradiation. These findings may establish a new avenue to inhibit the aggregation of amyloid peptide hIAPP and enrich the current selection of modulators. (C) 2017 Elsevier Inc. All rights reserved.

Original languageEnglish
JournalJournal of Colloid and Interface Science
Volume495
Pages (from-to)37-43
Number of pages7
ISSN0021-9797
DOIs
Publication statusPublished - 1 Jun 2017

Keywords

  • Scanning probe microscopy
  • Amyloid peptide aggregation
  • Nanomechanical mapping
  • Amyloid fibril
  • MECHANICAL-PROPERTIES
  • GRAPHENE OXIDE
  • BETA
  • AGGREGATION
  • NANOPARTICLES
  • INHIBITION
  • TOXICITY

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