Dependence of ethanol effects on protein charges

Shunsuke Yoshizawa; Tsutomu Arakawa; Kentaro Shiraki

doi:10.1016/j.ijbiomac.2014.04.041

Dependence of ethanol effects on protein charges

Int J Biol Macromol. 2014 Jul:68:169-72. doi: 10.1016/j.ijbiomac.2014.04.041. Epub 2014 Apr 26.

Authors

Shunsuke Yoshizawa¹, Tsutomu Arakawa², Kentaro Shiraki³

Affiliations

¹ Faculty of Pure and Applied Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8573, Japan.
² Alliance Protein Laboratories, San Diego, CA 92121, United States.
³ Faculty of Pure and Applied Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8573, Japan. Electronic address: shiraki@bk.tsukuba.ac.jp.

PMID: 24780565
DOI: 10.1016/j.ijbiomac.2014.04.041

Abstract

Ethanol is used as a conventional disinfectant solution. It is highly effective against enveloped viruses due to its effects on virus membranes. It also confers inactivation of non-enveloped viruses, which can be ascribed to conformational changes or changes in association state of the viral proteins induced by ethanol. We have examined here the effects of pH and hence the charged state of proteins on the ethanol-induced conformational changes and self-association of model proteins, i.e., bovine serum albumin (BSA) and ribonuclease A (RNase A). Both proteins showed qualitatively different aggregation behavior and structure changes by ethanol at pH 4.0 and 7.0, at which BSA has opposite charges and RNase A has different degree of net positive charges.

Keywords: Charged state; Ethanol induced aggregation; Protein.

MeSH terms

Animals
Cattle
Circular Dichroism
Ethanol / pharmacology*
Hydrogen-Ion Concentration
Ribonuclease, Pancreatic / chemistry*
Serum Albumin, Bovine / chemistry*

Substances

Serum Albumin, Bovine
Ethanol
Ribonuclease, Pancreatic