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ISSN: 1023-5086


ISSN: 1023-5086

Scientific and technical

Opticheskii Zhurnal

A full-text English translation of the journal is published by Optica Publishing Group under the title “Journal of Optical Technology”

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DOI: 10.17586/1023-5086-2020-87-06-34-42

Characterization of interaction between ligustroflavone and bovine serum albumin

For Russian citation (Opticheskii Zhurnal):

Sun S., Yuan Z., Lu Y.Q. Характеризация взаимодействия лигустрофлавона с бычьим сывороточным альбумином // Оптический журнал. 2020. Т. 87. № 6. С. 34–42.


Sun S., Yuan Z., Lu Y.Q. Characterization of interaction between ligustroflavone and bovine serum albumin [in English] // Opticheskii Zhurnal. 2020. Т. 87. № 6. С. 34–42.

For citation (Journal of Optical Technology):
S. Sun, Z. Yuan, and Y. Q. Lu, "Characterization of the interaction between ligustroflavone and bovine serum albumin," Journal of Optical Technology. 87(6), 349-354 (2020).

The interaction of ligustroflavone with bovine serum albumin was investigated by affinity capillary electrophoresis, ultraviolet visible absorption spectroscopy and fluorescence quenching methods in this ariticle. The affinity capillary electrophoresis gives binding constants (Ka) at near-physiological conditions. Mobility ratio (M) was selected to deduce the Ka, which effectively eliminates the influence of electroosmotic flow. The fluorescence quenching method provided quenching constant Ksv, binding site number n and binding constants Kb. The fluorescence results indicate that bovine serum albumin fluorescence quenching is mainly a static quenching process. The Ka value (7.1089ґ104) obtained from affinity capillary electrophoresis is in agreement with Kb (value is 8.0057ґ104) from fluorescence spectroscopy showing ligustroflavone has great affinity toward bovine serum albumin. Complex formed between ligustroflavone and bovine serum albumin was evident from the data of ultraviolet visible absorption spectroscopy which is consistent with the fluorescence static quenching result. And thermodynamic parameters of the negative DH and DS values obtained by affinity capillary electrophoresis showed that the van der Waals interactions and hydrogen bond played important roles in the binding of ligustroflavone to bovine serum albumin. The data obtained in this paper can help us in gaining some insights on a possible drug/protein interaction.


ligustroflavone, bovine serum albumin, affinity capillary electrophoresis, fluorescence spectroscopy, binding constants, thermodynamic parameters

OCIS codes: 300.0300, 300.6280, 300.6540, 300.6550, 000.1430, 000.6850


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