A Thermodynamic Study on the Binding of PEG-Stearic Acid Copolymer with Lysozyme

被引：17

作者：

Behbehani, G. Rezaei ^{[1
]}

Divsalar, A. ^{[2
,3
]}

Saboury, A. A. ^{[2
]}

Hekmat, A. ^{[2
]}

机构：

[1] Imam Khomeini Int Univ, Dept Chem, Qazvin, Iran

[2] Univ Tehran, Inst Biochem & Biophys, Tehran, Iran

[3] Tarbiat Moallem Univ, Dept Biol Sci, Tehran, Iran

来源：

JOURNAL OF SOLUTION CHEMISTRY | 2009年 / 38卷 / 02期

关键词：

Lysozyme; Polyethyleneglycol-stearic acid; Isothermal titration calorimetry; Overall cooperativity; EGG-WHITE LYSOZYME; AQUEOUS-METHANOL; SERUM-ALBUMIN; PROTEIN; WATER; ENTHALPIES; POLYMERS; ACETONITRILE; REPRODUCE; MIXTURES;

D O I：

10.1007/s10953-008-9360-5

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

The thermodynamics of the interaction between a copolymer of polyethyleneglycol400-stearic acid, S400, and lysozyme was investigated at pH=7.0 and 27 A degrees C in phosphate buffer by isothermal titration calorimetry, ITC. The extended solvation model was used to reproduce the enthalpies of the S400 + lysozyme interactions. The solvation parameters recovered from the extended solvation model are attributed to the structural change of lysozyme and its biological activity. The binding parameters found for the interaction of S400 with lysozyme indicate that at low concentrations of S400, the lysozyme structure was destabilized but at higher concentrations of S400 lysozyme it was stabilized by S400. It is suggested that S400 interacts with a set of three identical binding sites on lysozyme.

引用

页码：219 / 229

页数：11

共 53 条

[1]

ASHBROOK JD, 1975, J BIOL CHEM, V250, P2333

[2]

BAHT R, 1992, PROTEIN SCI, V1, P1133

[3] Enthalpies of transfer of acetonitrile from water to aqueous methanol, ethanol and dimethylsulphoxide mixtures at 298.15 K [J].