Ten to fourteen residue peptides of Alzheimer's disease protein are sufficient for amyloid fibril formation and its characteristic xray diffraction pattern

PD Gorevic, EM Castano, R. Sarma, B. Frangione

Research output: Contribution to journalArticlepeer-review

147 Scopus citations

Abstract

The molecular basis of fibril formation in Alzheimers disease was explored by electron micrographic and x-ray diffraction analysis of a series of synthetic peptides corresponding to portions of the amino acid sequence of beta protein and that of its putative precursor. A minimum 14 residue peptide was identified that formed typical amyloid fibrils under physiological conditions. Of these 14 residues, 10 were sufficient to give an identical 4.76 A and 10.6 A diffraction pattern as that recently described for isolated neurofibrillary tangles, amyloid plaque cores and leptomeningeal amyloid fibrils.

Original languageEnglish
Pages (from-to)854-862
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume147
Issue number2
DOIs
StatePublished - 15 Sep 1987
Externally publishedYes

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