Nuclear Science and Techniques

《核技术》(英文版) ISSN 1001-8042 CN 31-1559/TL     2019 Impact factor 1.556

Nuclear Science and Techniques ›› 2016, Vol. 27 ›› Issue (5): 109 doi: 10.1007/s41365-016-0123-5

• NUCLEAR PHYSICS AND INTERDISCIPLINARY RESEARCH • Previous Articles     Next Articles

A facile and precise method for quantifying small–large/lightweighted molecular interaction system

Wan-Rong Li, Pei Gong, Yu-Xing Ma, Hai-Yang Gao, Xiao-Ling Yun, Ming Yuan, Yu-Shuang Liu, Feng Zhang   

  1. Agricultural Nanocenter, School of Life Sciences, Inner Mongolia Agricultural University, 306 Zhaowuda Road, Hohhot 010018, China
  • Contact: Feng Zhang E-mail:fengzhang1978@hotmail.com
  • Supported by:

    This work was supported by the National Natural Science Foundation of China (Nos. 21171086 and 81160213), the Inner Mongolia Autonomous Region science and Technology Department (No. 211-202077), the Inner Mongolia Grassland Talent (No. 108-108038), the Natural Science Foundation of Inner Mongolia Autonomous Region of China (Nos. 2013MS1121, 2015ms0806 and 2016MS0211) and the Inner Mongolia Agricultural University (Nos. 109-108040, 211-109003 and 211-206038).

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Wan-Rong Li, Pei Gong, Yu-Xing Ma, Hai-Yang Gao, Xiao-Ling Yun, Ming Yuan, Yu-Shuang Liu, Feng Zhang. A facile and precise method for quantifying small–large/lightweighted molecular interaction system.Nuclear Science and Techniques, 2016, 27(5): 109     doi: 10.1007/s41365-016-0123-5
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Abstract:

It is significant to quantify the intermolecular physisorption extent in biomedical field. By taking the advantage of a significant difference from either sizes or weights, we introduced a combination of Scatchard equation and either ultracentrifugation or size exclusion chromatography to obtain both the binding constant and the number of binding sites by using bovine serum albumin and eosin B as models. Compared to the photoluminescence quenching-based methods like Stern–Volmer and Hill equations, the introduced method is not only more precise but also simpler and more straightforward for the operation. Moreover, the protein conformational changes and the corresponding theoretical binding mode with an atomic resolution were also studied by using three-dimensional fluorescence spectroscopy and molecular docking method, respectively. These comparative results could help scientists select right methods to study any interactions between two molecules with significant differences from either sizes or weights.

Key words: Bovine serum albumin, Eosin B, Binding constant, Ultracentrifugation, Scatchard equation, Size exclusion chromatography