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

Citation
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
Citations number
19
Categorie Soggetti
Neurosciences
Journal title
ISSN journal
03043940
Volume
251
Issue
1
Year of publication
1998
Pages
65 - 68
Database
ISI
SICI code
0304-3940(1998)251:1<65:TIEOLA>2.0.ZU;2-M
Abstract
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.