RIFAMPICIN PREVENTS THE AGGREGATION AND NEUROTOXICITY OF AMYLOID-BETAPROTEIN IN-VITRO

The aggregation and cerebral deposition of amyloid beta protein (AP), which is a major component of senile plaques in Alzheimer's disease (A D) brains, is believed to be involved in the pathogenesis of AD. Inhib ition of A beta aggregation would seem to be a promising strategy for the treatment of AD. Here, we show that rifampicin, which is an antibi otic widely used in the treatment of tuberculosis and leprosy, inhibit ed the aggregation and fibril formation of synthetic A beta 1-40 pepti de in a dose-dependent manner at reasonable concentrations. Furthermor e, rifampicin was found to prevent A beta 1-40-induced neurotoxicity o n rat pheochromocytoma PC12 cells. Rifampicin may have therapeutic pot ential as an agent for inhibiting the initial step of amyloid formatio n in AD. (C) 1994 Academic Press, Inc.