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Article

Amyloidogenic Mutation Promotes Fibril Formation of the N-terminal Apolipoprotein A-I on Lipid Membranes.

The Journal of biological chemistry - 21 Aug 2015

Mizuguchi Chiharu, Ogata Fuka, Mikawa Shiho, Tsuji Kohei, Baba Teruhiko, Shigenaga Akira, Shimanouchi Toshinori, Okuhira Keiichiro, Otaka Akira, Saito Hiroyuki

Abstract excerpt

The N-terminal amino acid 1-83 fragment of apolipoprotein A-I (apoA-I) has a strong propensity to form amyloid fibrils at physiological neutral pH. Because apoA-I has an ability to bind to lipid membranes, we examined the effects of the lipid environment on fibril-forming properties of the N-terminal fragment of apoA-I variants. Thioflavin T fluorescence assay as well as fluorescence and transmission microscopies...

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Identifiers

PMID: 26175149
DOI: 10.1074/jbc.M115.664227
PMCID: PMC4543654

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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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