Tomiyama T, Asano S, Suwa Y, Morita T, Kataoka K, Mori H, Endo N
Teijin Institute for Biomedical Research, Tokyo, Japan.
Biochem Biophys Res Commun. 1994 Oct 14;204(1):76-83. doi: 10.1006/bbrc.1994.2428.
The aggregation and cerebral deposition of amyloid beta protein (A beta), which is a major component of senile plaques in Alzheimer's disease (AD) brains, is believed to be involved in the pathogenesis of AD. Inhibition of A beta aggregation would seem to be a promising strategy for the treatment of AD. Here, we show that rifampicin, which is an antibiotic widely used in the treatment of tuberculosis and leprosy, inhibited the aggregation and fibril formation of synthetic A beta 1-40 peptide in a dose-dependent manner at reasonable concentrations. Furthermore, rifampicin was found to prevent A beta 1-40-induced neurotoxicity on rat pheochromocytoma PC12 cells. Rifampicin may have therapeutic potential as an agent for inhibiting the initial step of amyloid formation in AD.
淀粉样β蛋白（Aβ）是阿尔茨海默病（AD）大脑中老年斑的主要成分，其聚集和脑内沉积被认为与AD的发病机制有关。抑制Aβ聚集似乎是治疗AD的一种有前景的策略。在此，我们表明，利福平是一种广泛用于治疗结核病和麻风病的抗生素，在合理浓度下以剂量依赖的方式抑制合成的Aβ1-40肽的聚集和纤维形成。此外，发现利福平可预防Aβ1-40对大鼠嗜铬细胞瘤PC12细胞的神经毒性。利福平作为一种抑制AD中淀粉样蛋白形成初始步骤的药物可能具有治疗潜力。
