The inhibitory effect of laminin 1 and synthetic peptides deduced from the sequence in the laminin alpha1 chain on Abeta40 fibril formation in vitro.
We investigated whether or not laminin 1 and the two different synthetic peptides deduced from the sequence in the laminin alphal chain, both of which mediate cell attachment and neurite outgrowth in PC12 cells, have an effect on Abeta40 fibril formation in vitro. A thioflavine-T fluorometric assay showed a synthetic peptide containing the YFQRYLI sequence from the laminin alpha1 chain to inhibit Abeta40 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 alpha1 chain may thus be an effective therapeutic agent for either preventing or slowing down the progression of amyloidogenesis in Alzheimer's disease.
Department of Neuropsychiatry, Faculty of Medicine, Kyushu University, Fukuoka, Japan.
A
A
Monji
K
K
Tashiro
Y
Y
Hayashi
I
I
Yoshida
N
N
Tashiro
D000595:Amino Acid Sequence; D016229:Amyloid beta-Peptides / Q000187:drug effects / Q000648:ultrastructure*; D000818:Animals; D007797:Laminin / Q000737:chemistry / Q000494:pharmacology / Q000502:physiology*; D008854:Microscopy, Electron; D016716:PC12 Cells; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000187:drug effects / Q000494:pharmacology* / Q000648:ultrastructure*; D051381:Rats
D016229:Amyloid beta-Peptides; D007797:Laminin; D010446:Peptide Fragments; C078592:amyloid beta-protein (1-40); C084098:laminin A