A supramolecular route for reversible protein-polymer conjugation

被引：100

作者：

Biedermann, Frank ^{[1
]}

Rauwald, Urs ^{[1
]}

Zayed, Jameel M. ^{[1
]}

Scherman, Oren A. ^{[1
]}

机构：

[1] Univ Cambridge, Dept Chem, Melville Lab Polymer Synth, Cambridge CB2 1EW, England

来源：

CHEMICAL SCIENCE | 2011年 / 2卷 / 02期

基金：

英国工程与自然科学研究理事会;

关键词：

BOVINE SERUM-ALBUMIN; LIVING RADICAL POLYMERIZATION; SITE-SPECIFIC PEGYLATION; POLYETHYLENE-GLYCOL; MOLECULAR PRINTBOARDS; THERAPEUTIC PROTEINS; COVALENT ATTACHMENT; HOST; BINDING; CHEMISTRY;

D O I：

10.1039/c0sc00435a

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The supramolecular formation of a PEGylated bovine serum albumin (BSA) protein-polymer bioconjugate in water has been demonstrated through a selective host-guest interaction with the macrocycle cucurbit[8]uril (CB[8]). Both BSA and poly(ethylene glycol) were functionalised with either an electron-deficient first guest viologen or an electron-rich second guest naphthalene for the formation of the CB[8] ternary complex. With the help of spectroscopic (NMR, DOSY-NMR, DLS, UV/vis, fluorescence) and calorimetric (ITC) techniques, it was shown that a strong and specific binding interaction took place between the complementary labeled polymer and protein only in the presence of the macrocyclic host CB[8]. Moreover, we demonstrated that controlled formation of a supramolecular protein-protein complex was also possible through the use of CB[8] ternary formation.

引用

页码：279 / 286

页数：8

共 84 条

[1] Structural background of cyclodextrin-protein interactions [J].