RAFT polymers for protein recognition

Beilstein Journal of Organic Chemistry

Julia Liese¹  Arno Kraft¹  Alan F. Tominey¹  Klaus Kowski²  Thomas Schrader²  Sun Wei² 

[1] Chemistry, School of Engineering & Physical Sciences, Heriot-Watt University, Riccarton, Edinburgh EH14 4AS, United Kingdom;Universität Duisburg-Essen, Fachbereich Chemie, Institut für Organische Chemie, Universitätsstraße 5, 45117 Essen, Germany;

关键词: electrostatic interactions;    hydrophobic effect;    isothermal calorimetry;    protein recognition;    RAFT polymers;   

DOI  :  10.3762/bjoc.6.66

来源: DOAJ

【 摘 要 】

A new family of linear polymers with pronounced affinity for arginine- and lysine-rich proteins has been created. To this end, N-isopropylacrylamide (NIPAM) was copolymerized in water with a binding monomer and a hydrophobic comonomer using a living radical polymerization (RAFT). The resulting copolymers were water-soluble and displayed narrow polydispersities. They formed tight complexes with basic proteins depending on the nature and amount of the binding monomer as well as on the choice of the added hydrophobic comonomer.

【 授权许可】

Unknown