Methyl cyanide induces alpha to beta transition and aggregation at high concentrations in E-state of human serum albumin
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Updated: Jun 14, 2026

Preparation and In Vivo Use of an Activity-based Probe for N-acylethanolamine Acid Amidase
Published on: November 23, 2016
1Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, India.
Abstract:
We have studied the effect of 2,2,2-trifluoroethanol (TFE), an alpha-helix inducer, versus methyl cyanide (MeCN), a beta-sheet inducer, on acid-denatured human serum albumin (HSA) using far-UV circular dichroism, intrinsic fluorescence, 1-anilino-8-naphthalene sulfonate binding, and acrylamide quenching studies. Interestingly, at pH 2.0, where the recovery and resolution of the protein in reverse phase chromatography is high, its secondary structure remains unchanged even in the presence of very high concentration (76% v/v) of MeCN. Gain of 23 and 34% alpha-helicity was observed in the presence of 20 and 50% TFE, respectively. At pH 7.3, HSA aggregates in the presence of 40% MeCN, but it remains soluble up to 75% MeCN at pH 2.0. The results seem to be important for HSA isolation and purification.
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