Kinetics and Thermodynamics of 1-anilino-8-naphthalene Sulfonate Interactions with Urinary Trypsin Inhibitor

被引：3
|
作者：
Zuo, Zhenyu [1 ]
Fan, Handong
Guo, Jianjun
Zhou, Wei [1 ]
Li, Lingling [1 ]
机构：
[1] Wuhan Univ Sci & Technol, Coll Chem Engn & Technol, Wuhan 430081, Peoples R China
来源：
PROTEIN JOURNAL | 2012年 / 31卷 / 07期
关键词：
Urinary trypsin inhibitor; 1-Anilino-8-naphthalene sulfonate; Fluorescence spectrum; Isothermal titration calorimetry; Molecular modeling; OVARIAN-CANCER CELLS; BINDING; PROTEIN; STABILITY; ACID;
D O I：
10.1007/s10930-012-9443-4
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：
The interactions between Urinary Trypsin Inhibitor (UTI) and 1-anilino-8-naphthalene sulfonate (ANS) were investigated by fluorescence spectra, isothermal titration calorimetry and molecular modeling. The results revealed the presence of four specific binding sites for ANS on UTI, with interactions driven mainly by electrostatic forces. The four specific binding sites indicated the involvement of four hydrophobic patches on UTI. Experimental data also confirmed the presence of a further five nonspecific binding sites that interacted mainly by the formation of salt bridges between the sulfonates of ANS and positive residues on the surface of UTI.
引用
收藏
页码：585 / 591
页数：7
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