Relationship between surface hydrophilicity of a protein and its stability against denaturation by organic solvents.
The stability of alpha-chymotrypsin covalently modified with a strongly hydrophilic modifier, pyromellitic dianhydride, against solvent-induced denaturation in water-organic solvent binary mixtures has been studied. It was found that the hydrophilization results in a strong stabilization of the enzyme against denaturation by organic solvents. The stabilizing effect is explained in terms of the enhanced ability of the hydrophilized enzyme to keep its hydration shell, which is indispensable for supporting the native protein conformation, from denaturing stripping by organic solvents.
Khmelnitsky
Y L
YL
A.N. Bakh Institute of Biochemistry, Moscow, USSR.
Belova
A B
AB
Levashov
A V
AV
Mozhaev
V V
VV
D001565:Benzoates / Q000494:pharmacology; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002918:Chymotrypsin / Q000737:chemistry*; D004355:Drug Stability; D000432:Methanol / Q000494:pharmacology; D015394:Molecular Structure; D011489:Protein Denaturation; D012996:Solutions; D012997:Solvents; D013816:Thermodynamics; D014867:Water
D001565:Benzoates; D012996:Solutions; D012997:Solvents; D014867:Water; C012019:pyromellitic dianhydride; D002918:Chymotrypsin; D000432:Methanol