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Article

An early folding contact between Phe19 and Leu34 is critical for amyloid-β oligomer toxicity.

ACS chemical neuroscience - 19 Aug 2015

Das Anand K, Rawat Anoop, Bhowmik Debanjan, Pandit Rucha, Huster Daniel, Maiti Sudipta

Abstract excerpt

Small hydrophobic oligomers of aggregation-prone proteins are thought to be generically toxic. Here we examine this view by perturbing an early folding contact between Phe19 and Leu34 formed during the aggregation of Alzheimer's amyloid-β (Aβ40) peptide. We find that even conservative single mutations altering this interaction can abolish Aβ40 toxicity. Significantly, the mutants are not distinguishable either by...

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PMID: 25951510
DOI: 10.1021/acschemneuro.5b00074

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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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