The Interaction of HIV-1 Inhibitor 3,3',3'',3'''-Ethylenetetrakis-4-Hydroxycoumarin with Bovine Serum Albumin at Different pH
- Release time:2024-08-09
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Affiliation of Author(s):
化学与化工学院
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Journal:
Bull. Korean Chem. Soc.
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Key Words:
中文关键字：牛血清白蛋白；相互作用；光谱法，英文关键字：Bovine serum albumin (BSA); Interaction; Spectrome
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Abstract:
We studied the interaction of 3,3′,3′′,3′′′–ethylenetetrakis–4–hydroxycoumarin (EHC) with bovine serum albumin (BSA) in acetate buffer and phosphate buffer with different pH values by UV–vis absorption spectrometry and fluorescence spectrometry respectively. It was found that the pH values of the buffer solutions had an effect on the interaction process. In acetate buffer of pH 4.70, the carbonyl groups in EHC bound to the amino groups in BSA by means of hydrogen bond and van der Waals force, which made the extent of peptide chain in BSA changed. By contrast, in phosphate buffer of pH 7.40, hydrophobic force played a major role in the interaction between EHC and BSA, while the hydrogen bond and van der Waals force were also involved in the interaction. The results of spectrometry indicated that BSA could enhance the fluorescence intensity of EHC by forming a 1:1 EHC–BSA fluorescent complex through static mechanism at pH 4.70 and 7.40 respectively. Furthermore, EHC bound on site Ⅰ in BSA.
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Note:
董社英
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First Author:
dongsheying
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Indexed by:
Journal paper
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Volume:
卷：32
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Issue:
期：
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Page Number:
页：2949-2954
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Translation or Not:
no
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Date of Publication:
2011-06-01
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