Quantitative analysis of EGFR affinity to immobilized glycolipids by surface plasmon resonance

被引：6

作者：

Haga, Yoshimi ^{[1
]}

Hakomori, Sen-itiroh ^{[2
,3
]}

Hatanaka, Kenichi ^{[1
]}

机构：

[1] Univ Tokyo, Inst Ind Sci, Meguro Ku, Tokyo 1538505, Japan

[2] Pacific NW Res Inst, Seattle, WA 98122 USA

[3] Univ Washington, Dept Microbiol, Seattle, WA 98195 USA

来源：

CARBOHYDRATE RESEARCH | 2008年 / 343卷 / 18期

基金：

日本学术振兴会;

关键词：

Glycolipid; Lyso-GM3; mimetic; Epidermal growth factor receptor; Surface plasmon resonance; Dissociation rate constants; Association rate constants;

D O I：

10.1016/j.carres.2008.09.002

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

EGF-induced activation of EGFR tyrosine kinase is known to be inhibited by ganglioside GM3, its dimer, and other mimetics. However, details of the interaction, such as kinetic properties, have not yet been clarified. The direct interaction is now defined by the surface plasmon resonance (SPR) technique. To determine the affinity of EGFR for lyso-GM3 or lyso-GM3 mimetic, these glycolipid ligands were covalently immobilized onto a sensor chip, and binding affinities were investigated. Results of these studies confirmed the direct interaction of lyso-GM3 or its mimetic with EGFR. A strong interaction between EGFR and lyso-GM3 or its mimetic was indicated by increased binding of EGFR to glycolipid-immobilized surface, in an EGFR dose-dependent manner. (C) 2008 Elsevier Ltd. All rights reserved.

引用

页码：3034 / 3038

页数：5

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