Y10W β(1-40) fluorescence reflects epitope exposure in conformers of Alzheimer's β-peptide

Harry LeVine

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

The Alzheimer's β-peptide in neutral aqueous solution is characterized variously as a random coil or a heterogeneous mixture of conformers. Under conditions of lowered pH characteristic of intracellular compartments such as endosomes or lysosomes, a different conformation is favored, which is reflected in the biophysical and biological properties of the peptide. The reactivity of the epitope of the monoclonal antibody 6F/3D, encompassing residues 9-14, is drastically reduced. The fluorescence of human sequence β(1-40) with the tyrosine at position 10 substituted with tryptophan (Y10W β(1-40)) is quenched nearly 50% when the peptide is shifted to pH 4.6. The exposure of the 6F/3D epitope parallels Y10W β(1-40) fluorescence changes induced by a variety of perturbations. The linkage of the sensitivity of immunological detection with the potential for monitoring rapid changes by fluorescence offers convergence of biology and biophysics in the study of β-amyloid peptide conformation.

Original languageEnglish
Pages (from-to)112-122
Number of pages11
JournalArchives of Biochemistry and Biophysics
Volume417
Issue number1
DOIs
StatePublished - Sep 1 2003

Bibliographical note

Funding Information:
Funding for this work was provided by the Sanders-Brown Center on Aging and the Chandler Medical Center of the University of Kentucky.

Keywords

  • 6F/3D
  • Antibody
  • Conformation
  • ELISA
  • Epitope
  • Fluoroalcohol
  • PH
  • Trimethylamine-N-oxide
  • Tryptophan fluorescence

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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