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Article

Conformational dynamics of amyloid beta-protein assembly probed using intrinsic fluorescence.

Biochemistry - 11 Oct 2005

Maji Samir K, Amsden Jason J, Rothschild Kenneth J, Condron Margaret M, Teplow David B

Abstract excerpt

Formation of toxic oligomeric and fibrillar structures by the amyloid beta-protein (Abeta) is linked to Alzheimer's disease (AD). To facilitate the targeting and design of assembly inhibitors, intrinsic fluorescence was used to probe assembly-dependent changes in Abeta conformation. To do so, Tyr was substituted in Abeta40 or Abeta42 at position 1, 10 (wild type), 20, 30, 40, or 42. Fluorescence then was...

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PMID: 16201761
DOI: 10.1021/bi0508284

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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