albumin - publications

Predict more albumin - ligand interactions now!

1. Int J Biol Macromol. 2012 Mar 30. [Epub ahead of print]

Effects of alcohol on the solubility and structure of native and
disulfide-modified bovine serum albumin.

Yoshikawa H, Hirano A, Arakawa T, Shiraki K.

Faculty of Pure and Applied Science, University of Tsukuba, Tsukuba, Ibaraki
305-8573, Japan.

Differential precipitation of human plasma by ethanol is one of the most
important processes for purifying therapeutic proteins, including human serum
albumin. Better understanding of the effects of ethanol on the structure and
stability of proteins is critical for effective and safe application of
ethanol-induced protein precipitation. Here, we examined the effects of ethanol
on the structure and solubility of bovine serum albumin (BSA) and SH-modified
BSA. Ethanol caused BSA denaturation in a bimodal fashion, i.e., reduction of
α-helix at low concentration and subsequent induction of the α-helical structure
at higher concentration. In contrast, the solubility of BSA decreased
monotonically. The secondary structure of SH-modified BSA was different from that
of native BSA. Ethanol resulted in enhanced secondary structures of SH-modified
BSA and decreased solubility monotonically. These results suggest the favorable
interaction of ethanol with hydrophobic residues, leading to protein
denaturation, but the unfavorable interaction with charged residues, leading to a
reduction of protein solubility.

Copyright © 2012. Published by Elsevier B.V.

PMID: 22484442 [PubMed - as supplied by publisher]