Poly-L-lysine dissolves fibrillar aggregation of the Alzheimer beta-amyloid peptide in vitro.
beta-Amyloid peptide (beta A) is a major fibrillar component of neuritic plaques in Alzheimer's disease (AD) brains and is related to the pathogenesis of the disease. In this study, using electron microscopy, we describe herein the results concerning the efficacy of compounds that can dissolve preformed beta A fibrils in vitro. For such a purpose, two hydrosoluble and biocompatible polymers such as polyethylene glycol and poly-L-lysine were used. The poly-L-lysine appears as a potent dissolver of preformed beta A fibrils in vitro. Its efficiency is instantaneous. Poly-L-lysine can be used as a universal dissolver of all types of oligomeric beta-sheet conformation, precursor of the fibrils. This finding provides the basis for future investigation of the therapeutic potential of poly-L-lysine in terms of preventing and/or retarding amyloidogenesis in AD and other types of amyloid-related disorders.
Nguyen
Khue Vu
KV
CNRS FRE 2168, Laboratoire des Mécanismes Moléculaire de la Division Cellulaire et du Développement, 15 rue René Descartes, 67084 Strasbourg Cédex, France. kv52nguyen@yahoo.com
Gendrault
Jean-Louis
JL
Wolff
Charles-Michel
CM
D000544:Alzheimer Disease / Q000473:pathology; D016229:Amyloid beta-Peptides / Q000187:drug effects* / Q000648:ultrastructure*; D000818:Animals; D011092:Polyethylene Glycols / Q000494:pharmacology; D011107:Polylysine / Q000494:pharmacology*
D016229:Amyloid beta-Peptides; D011107:Polylysine; D011092:Polyethylene Glycols