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Study on the Mechanism of Interaction Between Tubeimoside I and Human Serum Albumin at Different Temperatures by Three-Dimensional Fluorescence Spectrum

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Abstract

Tubeimoside (TBMS), the bulb of Bolbostemma paniculatum (Maxim.) Franquet (Cucurbitaceae), is one of the traditional Chinese medicines often used for the treatment of tumors as well as for detoxication. Tubeimoside I (TBMS I) is one of the main active ingredients of TBMS, the mechanism of action of which remains unknown. Human serum albumin (HSA) is the most abundant carrier protein in blood circulation. Three-dimensional (3D) fluorescence spectra and the excitation–emission matrix of interaction between TBMS I and HSA were measured at different temperatures. The results showed that HSA fluorescence was quenched by TBMS I through a static quenching mechanism. Also, the HSA fluorescence was quenched with the temperature increase from 283 K to 353 K. 3D spectral results revealed the changes in the secondary structure of HSA upon interaction with TBMS I.

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Acknowledgments

This work was supported by the National Natural Science Foundation of China (No. 61377001), and the Fundamental Research Funds for the Central Universities (Nos. CDJZR12125501 and 10611201312011).

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Authors and Affiliations

  1. Key Laboratory of Optoelectronic Technology and Systems, Ministry of Education, College of Optoelectronic Engineering, Chongqing University, Chongqing, 400030, China

    Xiaogang Lin, Wenchao Li, Changbin Ye & Zhiyuan Liu

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  1. Xiaogang Lin
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  2. Wenchao Li
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  3. Changbin Ye
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  4. Zhiyuan Liu
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Correspondence to Xiaogang Lin.

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Lin, X., Li, W., Ye, C. et al. Study on the Mechanism of Interaction Between Tubeimoside I and Human Serum Albumin at Different Temperatures by Three-Dimensional Fluorescence Spectrum. Int J Thermophys 36, 919–923 (2015). https://doi.org/10.1007/s10765-014-1657-6

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  • DOI: https://doi.org/10.1007/s10765-014-1657-6

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