2,2,2-Trifluroethanol induces simultaneous increase in α-helicity and aggregation in alkaline unfolded state of bovine serum albumin

Little work has been done to understand the folding of proteins at alkaline conditions. BSA acquires a partially reversible unfolded state at pH 13 0, devoid of any native structure Introduction of methanol, ethanol and 2-propanol with the alkaline unfolded protein resulted in beta-sheet-like structure formation, and 2,2,2-trifluroethanol found to enhance a-helical conformations with simultaneous increase in aggregation The extent of secondary and tertiary structure formation is in the order of methanol < ethanol < 2-propanol < 2,2.2-trifluroethanol Exposure of hydrophobic core of protein molecules in apolar environment of 2,2.2-trifluroethanol seems to promote intermolecular cluster formation This is one of the very few reports that a-helical structures can also aggregate (C) 2010 Elsevier B V All rights reserved