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Article

Aggregation and metal-binding properties of mutant forms of the amyloid A beta peptide of Alzheimer's disease.

Journal of neurochemistry - 1 Feb 1996

Clements A, Allsop D, Walsh D M, Williams C H

Abstract excerpt

The fibrillogenic properties of Alzheimer's A beta peptides corresponding to residues 1-40 of the normal human sequence and to two mutant forms containing the replacement Ala21 to Gly or Glu22 to Gln were compared. At pH 7.4 and 37 degrees C the Gln22 peptide was found to aggregate and precipitate from solution faster than the normal A beta, whereas the Gly21 peptide aggregated much more slowly. Electron...

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Source

Identifiers

PMID: 8592147
DOI: 10.1046/j.1471-4159.1996.66020740.x

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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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