2,2,2-Trifluroethanol induces simultaneous increase in alpha-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 alpha-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 alpha-helical structures can also aggregate.
Sen
Priyankar
P
Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh-202002, India.
Ahmad
Basir
B
Rabbani
Gulam
G
Khan
Rizwan Hasan
RH
D000468:Alkalies / Q000494:pharmacology*; D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D000431:Ethanol / Q000494:pharmacology*; D005453:Fluorescence; D006863:Hydrogen-Ion Concentration / Q000187:drug effects; D017510:Protein Folding / Q000187:drug effects*; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012710:Serum Albumin, Bovine / Q000737:chemistry* / Q000378:metabolism*; D014270:Trifluoroethanol / Q000494:pharmacology*
D000468:Alkalies; D012710:Serum Albumin, Bovine; D000431:Ethanol; D014270:Trifluoroethanol