Molecular recognition force spectroscopy of a specific lectin-carbohydrate interaction at single-molecule level

被引：8
|
作者：
Li, Yongjun [1 ,2 ]
Qiao, Haiyan [1 ,2 ]
Xing, Chunyan [1 ,2 ]
Zhang, Jing [1 ,2 ]
Wang, Lai-Xi [3 ,4 ]
Wang, Hongda [1 ]
Zhang, Bailin [1 ]
Tang, Jilin [1 ]
机构：
[1] Chinese Acad Sci, Changchun Inst Appl Chem, State Key Lab Electroanalyt Chem, Changchun 130022, Peoples R China
[2] Chinese Acad Sci, Grad Sch, Beijing 100049, Peoples R China
[3] Univ Maryland, Sch Med, Inst Human Virol, Baltimore, MD 21201 USA
[4] Univ Maryland, Sch Med, Dept Biochem & Mol Biol, Baltimore, MD 21201 USA
来源：
JOURNAL OF STRUCTURAL BIOLOGY | 2011年 / 176卷 / 01期
基金：
美国国家科学基金会;
关键词：
Atomic force microscopy; Lectin; Carbohydrate; Molecular recognition force spectroscopy; Bovine asialofetuin; Ricinus communis agglutinin-120 (RCA(120)); S-LAYER NANOARRAYS; PROTEINS; AFFINITY; AFM; DNA; LOCALIZATION; ANTIBODIES; DEPENDENCE; KINETICS; RECEPTOR;
D O I：
10.1016/j.jsb.2011.05.018
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：
Carbohydrates are involved in many essential biological recognition processes in physiological and pathological states. Thus, it is important to understand the mechanism of protein-carbohydrate interactions at molecular level. In the present study, molecular recognition force spectroscopy was applied to investigate the interactions between RCA(120), a lectin from Ricinus communis, and galactose (Gal) and asialofetuin (ASF) at the single-molecule level. RCA(120) coupled to the AFM tip could specifically recognize Gal and ASF, respectively. The unbinding forces of RCA(120)-Gal and RCA(120)-ASF increase linearly with the logarithm of loading rate. The results reveal that the binding capability of RCA(120) toward Gal is weaker than that of ASF, implicating a multivalent effect in the RCA(120)-ASF interaction. (C) 2011 Elsevier Inc. All rights reserved.
引用
收藏
页码：46 / 51
页数：6
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