Indispensable structure of solution additives to prevent inactivation of lysozyme for heating and refolding.
This article investigates solution additives that prevent misfolding of lysozyme from heating treatment and during refolding processes. Comparison of heat treatment of native lysozyme and oxidative refolding from the reduced and denatured state of lysozyme in the presence of 44 different additives revealed an indispensable chemical structure for the additives to be effective against heat-induced misfolding and for refolding. The additives effective against heat treatment of native lysozyme possessed a main chain of the amino acid moiety. Amino acids that have esterificated and amidated carboxy groups prevented heat-induced misfoldings more effectively than amino acids themselves. On the other hand, the additives effective against oxidative refolding possessed a guanidium or ureido group. The former additives prevented hydrophobic interaction between the main chains of the unfolded polypeptide, while the latter additives increased the solubility of the aromatic and aliphatic side-chains. These data also support the fact that arginine (Arg) and Arg derivatives are versatile additives for both misfolding processes.
Institute of Applied Physics, University of Tsukuba, Ibaraki, Japan.
Tsuneyoshi
T
Matsuoka
Hiroyuki
H
Hamada
Koji
K
Matsumoto
Kentaro
K
Shiraki
D000818:Animals; D001120:Arginine / Q000737:chemistry; D019791:Guanidine / Q000737:chemistry; D057927:Hydrophobic and Hydrophilic Interactions; D007700:Kinetics; D008956:Models, Chemical; D009113:Muramidase / Q000737:chemistry*; D010084:Oxidation-Reduction; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D055550:Protein Stability; D012995:Solubility; D012996:Solutions / Q000737:chemistry; D013696:Temperature
D012996:Solutions; D001120:Arginine; C421864:hen egg lysozyme; D009113:Muramidase; D019791:Guanidine