THE INHIBITORY EFFECT OF LAMININ-1 AND SYNTHETIC PEPTIDES DEDUCED FROM THE SEQUENCE IN THE LAMININ ALPHA-1 CHAIN ON A-BETA-40 FIBRIL FORMATION IN-VITRO
A. Monji et al., THE INHIBITORY EFFECT OF LAMININ-1 AND SYNTHETIC PEPTIDES DEDUCED FROM THE SEQUENCE IN THE LAMININ ALPHA-1 CHAIN ON A-BETA-40 FIBRIL FORMATION IN-VITRO, Neuroscience letters, 251(1), 1998, pp. 65-68
We investigated whether or not laminin 1 and the two different synthet
ic peptides deduced from the sequence in the laminin arl chain, both o
f which mediate cell attachment and neurite outgrowth in PC12 cells, h
ave an effect on A beta 40 fibril formation in vitro. A thioflavine-T
fluorometric assay showed a synthetic peptide containing the YFQRYLI s
equence from the laminin alpha 1 chain to inhibit A beta 40 fibril for
mation while the inhibitory effect of this peptide was found to be som
ewhat less than that of intact laminin 1. These results were confirmed
by electron microscopic observations using negative staining. The fin
dings of the present study suggested that the synthetic peptide derive
d from the laminin alpha 1 chain may thus be an effective therapeutic
agent for either preventing or slowing down the progression of amyloid
ogenesis in Alzheimer's disease. (C) 1998 Elsevier Science Ireland Ltd
. All rights reserved.