BINDING OF THERMO-SENSITIVE AND pH-SENSITIVE BUTYLATED POLY(ALLYLAMINE)S WITH LYSOZYME  

作　　者：姚萍 

机构地区：[1]Key Laboratory of Molecular Engineering of Polymer and Department of Macromolecular Science,Fudan University

出　　处：《Chinese Journal of Polymer Science》2011年第4期397-406,共10页高分子科学（英文版）

基　　金：supported by the National Natural Science Foundation of China(No.20874016);the innovative team of Ministry of Education of China(IRT0911);National Basic Research Program of China(973 Program 2009CB930402 and 2011CB932503)

摘　　要：Butyl modified poly（allylamine）s with butyl substitution degrees of 15% to 70% were prepared. The polymers show pH sensitive property and lower critical solution temperature （LCST） behavior. The LCST appears at lower temperature, lower pH and lower polymer concentration for the polymer with higher butylated degree. The binding of native lysozyme with the polymers depends on the hydrophobicity of the polymers at the pH range that the protein and the polymer carry the same positive charges. The increase of polymer hydrophobicity can increase the binding with lysozyme, but the self-aggregation of the polymer decreases the binding. The bound lysozyme molecules can recover their native activity completely after the dissociation of the complexes. Compared with native lysozyme, the denatured one which exposes the hydrophobic residues can increase the binding with the polymer and form stable complex nanoparticles.Butyl modified poly（allylamine）s with butyl substitution degrees of 15% to 70% were prepared. The polymers show pH sensitive property and lower critical solution temperature （LCST） behavior. The LCST appears at lower temperature, lower pH and lower polymer concentration for the polymer with higher butylated degree. The binding of native lysozyme with the polymers depends on the hydrophobicity of the polymers at the pH range that the protein and the polymer carry the same positive charges. The increase of polymer hydrophobicity can increase the binding with lysozyme, but the self-aggregation of the polymer decreases the binding. The bound lysozyme molecules can recover their native activity completely after the dissociation of the complexes. Compared with native lysozyme, the denatured one which exposes the hydrophobic residues can increase the binding with the polymer and form stable complex nanoparticles.

关 键 词：Hydrophobic interaction LCST Polyelectrolytes Protein binding. 

分 类 号：O631.3[理学—高分子化学]