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

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 b...

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Bibliographic Details
Published in:	高分子科学：英文版 Vol. 29; no. 4; pp. 397 - 406
Main Author:	Jing-jing Liu Yun-feng Yan Ping Yao
Format:	Journal Article
Language:	English
Published:	2011
Subjects:	pH敏感丁基化丙烯胺低临界溶解温度溶菌酶热敏感约束力聚合物浓度
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Summary:	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.
Bibliography:	Hydrophobic interaction; LCST; Polyelectrolytes; Protein binding. 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. 11-2015/O6
ISSN:	0256-7679 1439-6203