Abstract
We investigated whether or not laminin 1 and the two different synthetic peptides deduced from the sequence in the laminin α1 chain, both of which mediate cell attachment and neurite outgrowth in PC12 cells, have an effect on A β40 fibril formation in vitro. A thioflavine-T fluorometric assay showed a synthetic peptide containing the YFQRYLI sequence from the laminin α1 chain to inhibit A β40 fibril formation while the inhibitory effect of this peptide was found to be somewhat less than that of intact laminin 1. These results were confirmed by electron microscopic observations using negative staining. The findings of the present study suggested that the synthetic peptide derived from the laminin α1 chain may thus be an effective therapeutic agent for either preventing or slowing down the progression of amyloidogenesis in Alzheimer's disease.
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