Abstract
Laminin, an important extracellular matrix component is induced by brain injury and colocalizes with amyloid-β-peptide (Aβ) deposits in Alzheimer brains. We report here that laminin inhibits amyloid fibril formation as determined by thioflavin T fluorescence spectroscopy and electron microscopic examination. The inhibition of amyloid formation by laminin was concentration dependent and was observed at a laminin concentration of 300 nM, corresponding to a laminin/Aβ protein molar ratio of 1:800. The potential effect of laminin, may prove important to inhibit Aβ fibrillogenesis in vivo, specifically at the level of cerebral blood vessels.
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