Plasmin cleaves Aβ42 in vitro and prevents its aggregation into β-pleated sheet structuresExley, ChristopherCA; Korchazhkina, Olga V.1Neuroreport: September 17th, 2001 - Volume 12 - Issue 13 - p 2967-2970 Membrane And Cellular Biophysics And Biochemistry Abstract Author InformationAuthors The formation, aggregation and deposition of amyloid β peptide (Aβ) is implicated in the aetiology of Alzheimer's disease. Impairment of proteolytic degradation of Aβ may be a key factor in the progression of the disease. We have used RP-HPLC and thioflavin T fluorescence to demonstrate that Aβ42 is rapidly cleaved by the protease plasmin and that cleavage prevented the aggregation of Aβ42, and its cleavage products, into β-pleated sheet structures. Plasmin may fulfil a similar role in vivo. Birchall Centre for Inorganic Chemistry and Materials Science, School of Chemistry and Physics, and 1Centre for Science and Technology in Medicine, Keele University, Staffordshire, ST5 5BG, UK CACorresponding Author: email@example.com Received 13 June 2001; accepted 20 July 2001 © 2001 Lippincott Williams & Wilkins, Inc.