Laminin, an important extracellular matrix component is induced by bra
in injury and colocalizes with amyloid-beta-peptide (A beta) deposits
in Alzheimer brains. We report here that laminin inhibits amyloid fibr
il formation as determined by thioflavin T fluorescence spectroscopy a
nd electron microscopic examination. The inhibition of amyloid formati
on by laminin was concentration dependent and was observed at a lamini
n concentration of 300 nM, corresponding to a laminin/A beta protein m
olar ratio of 1:800. The potential effect of laminin, may prove import
ant to inhibit AP fibrillogenesis in vivo, specifically at the level o
f cerebral blood vessels.