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Article

Mechanism of IAPP amyloid fibril formation involves an intermediate with a transient β-sheet.

Proceedings of the National Academy of Sciences of the United States of America - 26 Nov 2013

Buchanan Lauren E, Dunkelberger Emily B, Tran Huong Q, Cheng Pin-Nan, Chiu Chi-Cheng, Cao Ping, Raleigh Daniel P, de Pablo Juan J, Nowick James S, Zanni Martin T

Abstract excerpt

Amyloid formation is implicated in more than 20 human diseases, yet the mechanism by which fibrils form is not well understood. We use 2D infrared spectroscopy and isotope labeling to monitor the kinetics of fibril formation by human islet amyloid polypeptide (hIAPP or amylin) that is associated with type 2 diabetes. We find that an oligomeric intermediate forms during the lag phase with parallel β-sheet...

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Share to Amyloid
Share to Islet Amyloid Polypeptide

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Molecular Dynamics Simulation

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Share to Spectrophotometry, Infrared

Source

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Identifiers

PMID: 24218609
DOI: 10.1073/pnas.1314481110
PMCID: PMC3845187

Genes

IAPP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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