Binding energetics of lysozyme to copolymers of N-isopropylacrylamide with sodium sulfonated styrene.
Interpolyelectrolyte complexes of lysozyme with thermosensitive N-isopropylacrylamide-sodium sulfonated styrene copolymers of different charge density were investigated by high-sensitivity differential scanning calorimetry (HS-DSC) at pH 4.6-7.2 and low ionic strength. A general property of the complexes for all copolymers investigated was a decrease in the conformational stability of the bound protein. This suggested the preferential binding of the unfolded protein to the polymer matrix. The isotherms of lysozyme binding to the copolymers were derived from the HS-DSC data. They indicate that the binding is irreversible and charge stoichiometric.
Burova
Tatiana V
TV
A.N. Nesmeyanov Institute of Organoelement Compounds, Russian Academy of Sciences, Vavilov St. 28, 119991 Moscow, Russian Federation. burova@ineos.ac.ru
Grinberg
Natalia V
NV
Grinberg
Valerij Ya
VY
Tang
Yecang
Y
Zhang
Guangzhao
G
Khokhlov
Alexei R
AR
D000178:Acrylamides / Q000378:metabolism*; D002152:Calorimetry, Differential Scanning; D007700:Kinetics; D009113:Muramidase / Q000378:metabolism*; D011108:Polymers / Q000378:metabolism*; D011137:Polystyrenes / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D011489:Protein Denaturation; D055550:Protein Stability; D012015:Reference Standards; D012996:Solutions; D013816:Thermodynamics; D044366:Transition Temperature
D000178:Acrylamides; D011108:Polymers; D011137:Polystyrenes; D012996:Solutions; C003321:polystyrene sulfonic acid; C067295:N-isopropylacrylamide; D009113:Muramidase