Fluorescence spectroscopy of osthole binding to human serum albumin

Guang-De Yang; Cong Li; Ai-Guo Zeng; Yuan Zhao; Rong Yang; Xiao-Li Bian

doi:10.1016/j.jpha.2012.10.002

Fluorescence spectroscopy of osthole binding to human serum albumin

J Pharm Anal. 2013 Jun;3(3):200-204. doi: 10.1016/j.jpha.2012.10.002. Epub 2012 Oct 23.

Authors

Guang-De Yang¹, Cong Li¹, Ai-Guo Zeng¹, Yuan Zhao², Rong Yang¹, Xiao-Li Bian¹

Affiliations

¹ School of Medicine, Xi'an Jiaotong University, No. 76 Yanta Westroad, Shaanxi Province, Xi'an 710061, PR China.
² Xi'an Tuberculosis and Thoracic Tumor Hospital, Shaanxi 710061, PR China.

Abstract

The interaction of human serum albumin (HSA) with osthole was investigated by fluorescence spectroscopy. Osthole can quench the fluorescence of HSA and the quenching mechanism is a static process. The binding site number n and apparent binding constant K were measured at different temperatures. The thermodynamic parameters ΔH⁰, ΔG⁰ and ΔS⁰ were calculated at different temperatures. The results indicated that electrostatic forces played a major role in the interaction of osthole with HSA. Results of osthole synchronous fluorescence and UV absorption spectra showed that the microenvironment and conformation of HSA were changed.

Keywords: Fluorescence quenching; Human serum albumin; Osthole.