期刊
JOURNAL OF MOLECULAR LIQUIDS
卷 219, 期 -, 页码 405-410出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.molliq.2016.03.040
关键词
Propofol; Human serum albumin; Fluorescence quenching; Circular dichroism; Site probing; Molecular docking
The interaction of human serum albumin (HSA) with propofol has been studied by fluorescence spectroscopy, Fourier transform infrared (FT-IR) spectroscopy, circular dichroism (CD) spectroscopy and docking methods. A gradual decrease in Stern-Volmer quenching constants with the increase in temperature showed the static mode of fluorescence quenching. The obtained binding constant (K-A) was 8.18 x 10(5) M-1. Gibbs free energy (Delta G), enthalpy (Delta H) and entropy (Delta S) changes were calculated, which revealed that the reaction is spontaneous, exothermic and hydrophobic force driven. FT-IR test revealed conformational changes of the protein and destruction of H-bonding upon interaction. Moreover, propofol induced a decrease in a-helical contents probably with increment of random coils or/and beta-sheets of HSA, as observed from the far-UV CD spectra. Molecular docking and site probing study depicted that propofol fits into the hydrophobic pocket close to Sudlow site I in domain IIA of HSA. The present study will be helpful in understanding the binding mechanism of propofol and associated stability and conformational changes. (C) 2016 Elsevier B.V. All rights reserved.
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