Multi-spectroscopic studies on the interaction of human serum albumin with astilbin: Binding characteristics and structural analysis

Wang, Jin; Li, Shuang; Peng, Xialian; Yu, Qing; Bian, He‐Dong; Huang, Fu‐Ping; Liang, Hong

doi:10.1016/j.jlumin.2012.12.004

Cited by 10 publications

(7 citation statements)

References 59 publications

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“…The reaction enthalpy change is regarded as a constant when the temperature hardly changes. Thus, the types of acting forces can be determined following Equations ( 3 and 4 ) as previously described [ 41 ].…”

Section: Methodsmentioning

confidence: 99%

Cordycepin and N6-(2-Hydroxyethyl)-Adenosine from Cordyceps pruinosa and Their Interaction with Human Serum Albumin

et al. 2015

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Cordyceps pruinosa (CP) is often used as Traditional Chinese Medicine, but the substance basis of its medicinal properties is unclear. In this study, two compounds were isolated from CP cultures by column chromatography, and identified as cordycepin and N6-(2-hydroxyethyl)-adenosine (HEA) by Nuclear Magnetic Resonance. In order to understand the efficacy of these two substances as potential therapeutic agents, it is necessary to explore their binding with proteins. The molecular mechanisms of interaction between cordycepin, HEA and human serum albumin (HSA) were studied using UV and fluorescence spectroscopy. The bingding constants between HSA and cordycepin were 4.227, 3.573 and 3.076 × 103·at 17, 27 and 37°C respectively, and that of HSA and HEA were 27.102, 19.409 and 13.002 × 103·at the three tempretures respectively. Both cordycepin and HEA can quench the intrinsic fluorescence of HSA via static quenching, and they can bind with HSA to form complexes with a single binding site. The interaction forces between cordycepin and HSA were determined as electrostatic and hydrophobic, and those of HEA and HSA were hydrogen bonding and van der Waals forces. Using Foster's equation, the distance between fluorophores of cordycepin and HSA, and HEA and HSA are estimated to be 5.31 nm and 4.98 nm, respectively. In this study, cordycepin was isolated for the first time from CP, and will provide a new source of cordycepin and expand the use of this taxon. The interaction mechanisms between cordycepin and HSA was studied for the first time, which will provide a useful guide for the clinical application of cordycepin. The pharmacological importance of this study is to understand the interaction of HSA with cordycepin and HEA, which will be essential for the future designing of drugs based on the two compounds.

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Section: Methodsmentioning

confidence: 99%

Cordycepin and N6-(2-Hydroxyethyl)-Adenosine from Cordyceps pruinosa and Their Interaction with Human Serum Albumin

et al. 2015

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“…To confirm the quenching mechanism induced by cefepime hydrochloride, fluorescence quenching data are analyzed with the Stern-Volmer equation (Equation 1) [26][27][28][29][30][31][32][33][34][35][36][37]:…”

Section: Resultsmentioning

confidence: 99%

Studies on the Interaction of Cefepime Hydrochloride with Bovine Serum Albumin by Fluorescence, Synchronous Fluorescence, Three-Dimensional Fluorescence and Circular Dichroism

Li¹

2017

J Bioanal Biomed

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“…In order to confirm the quenching mechanism, the fluorescence quenching was analyzed according to the well known Stern–Volmer equation: :

\frac{F_{0}}{F} = 1 + k_{q} τ_{0} ([], Q) = 1 + K_{s v} ([], Q)

where, F 0 and F are the fluorescence intensity in the absence and presence of the quencher, respectively, [ Q ] is the quencher concentration, and k q the quenching rate constant for a biomolecular reaction, K SV the Stern–Volmer quenching constant and τ 0 the average lifetime for fluorophore without quencher evaluated at 5 ns . Figure shows plots of F 0 / F versus isorhamnetin concentrations at different temperature and exhibits good linear correlations.…”

Section: Resultsmentioning

confidence: 99%

Investigation on the interaction between isorhamnetin and bovine liver catalase by spectroscopic techniques under different pH conditions

Yang

2016

Luminescence

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The binding of isorhamnetin to bovine liver catalase (BLC) was first investigated at 302, 310 and 318 K at pH 7.4 using spectroscopic methods including fluorescence spectra, circular dichroism (CD) and UV-vis absorption. Spectrophotometric observations are rationalized mainly in terms of a static quenching process. The binding constants and binding sites were evaluated by fluorescence quenching methods. Enzymatic activity of BLC in the absence and presence of isorhamnetin was measured using a UV/vis spectrophotometer. The result revealed that the binding of isorhamnetin to BLC led to a reduction in the activity of BLC. The positive entropy change and enthalpy change indicated that the interaction of isorhamnetin with BLC was mainly driven by hydrophobic forces. The distance r between the donor (BLC) and acceptor (isorhamnetin) was estimated to be 2.99 nm according to fluorescence resonance energy transfer. Fluorescence, synchronous fluorescence, and CD spectra showed no obvious change in the conformation of BLC upon the binding of isorhamnetin. In addition, the influence of pH on the binding of isorhamnetin to BLC was investigated and the binding ability of the drug to BLC deceased under other pH conditions (pH 9.0, 6.5, 5.0, 3.5, or 2.0) as compared with that at pH 7.4. Copyright © 2016 John Wiley & Sons, Ltd.

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Multi-spectroscopic studies on the interaction of human serum albumin with astilbin: Binding characteristics and structural analysis

Cited by 10 publications

References 59 publications

Cordycepin and N6-(2-Hydroxyethyl)-Adenosine from Cordyceps pruinosa and Their Interaction with Human Serum Albumin

Cordycepin and N6-(2-Hydroxyethyl)-Adenosine from Cordyceps pruinosa and Their Interaction with Human Serum Albumin

Studies on the Interaction of Cefepime Hydrochloride with Bovine Serum Albumin by Fluorescence, Synchronous Fluorescence, Three-Dimensional Fluorescence and Circular Dichroism

Investigation on the interaction between isorhamnetin and bovine liver catalase by spectroscopic techniques under different pH conditions

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