Self-assembly of polymer amphiphiles: Thermodynamics of complexation between bovine serum albumin and self-aggregate of cholesterol-bearing pullulan

被引：35

作者：

Akiyoshi, K

Nishikawa, T

Mitsui, Y

Miyata, T

Kodama, M

Sunamoto, J

机构：

[1] KYOTO UNIV,GRAD SCH ENGN,DEPT SYNTHET CHEM & BIOL CHEM,SAKYO KU,KYOTO 606,JAPAN

[2] OKAYAMA UNIV SCI,DEPT BIOCHEM,OKAYAMA 700,JAPAN

来源：

COLLOIDS AND SURFACES A-PHYSICOCHEMICAL AND ENGINEERING ASPECTS | 1996年 / 112卷 / 2-3期

关键词：

bovine serum albumin; cholesterol-bearing pullulan; hydrogel; hydrophobized pullulan; polymer amphiphile; self-assembly; thermodynamics;

D O I：

10.1016/0927-7757(96)03560-1

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 interaction between bovine serum albumin (BSA) and a hydrogel nanoparticle formed by the self-aggregation of cholesterol-bearing pullulan (CHP) was investigated by using an isothermal titration microcalorimeter. In water, one nanoparticle of the CHP self-aggregates strongly bound approximately one BSA molecule. The heats associated with the complexation were exothermic. The complexation is enthalpically, not entropically, driven. The negative enthalpy change for the complexation would be due mainly to the formation of direct or water-mediated hydrogen bonds formed between the protein and the polysaccharide skeleton of CHP.

引用

页码：91 / 95

页数：5

共 25 条

[1] SPECIFIC INTERACTIONS OF PROTEINS WITH FUNCTIONAL LIPID MONOLAYERS - WAYS OF SIMULATING BIOMEMBRANE PROCESSES [J].