Dependence of ethanol effects on protein charges.
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.
Faculty of Pure and Applied Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8573, Japan.
Shunsuke
S
Yoshizawa
Alliance Protein Laboratories, San Diego, CA 92121, United States.
Tsutomu
T
Arakawa
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.
Kentaro
K
Shiraki
D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D000431:Ethanol / Q000494:pharmacology*; D006863:Hydrogen-Ion Concentration; D012259:Ribonuclease, Pancreatic / Q000737:chemistry*; D012710:Serum Albumin, Bovine / Q000737:chemistry*
D012710:Serum Albumin, Bovine; D000431:Ethanol; D012259:Ribonuclease, Pancreatic
Charged state; Ethanol induced aggregation; Protein