Dataset Information

Insight into the binding interaction of kaempferol-7-O-?-L-rhamnopyranoside with human serum albumin by multiple fluorescence spectroscopy and molecular modeling.

ABSTRACT: Human serum albumin (HSA) is a transporting protein that has multiple functions. The binding interaction between HSA and small molecules affects its function and efficacy of small molecules. The present study reports that kaempferol-7-O-?-L-rhamnopyranoside (KR) interacts with HSA as indicated by multiple fluorescence spectroscopy and molecular modeling. KR can quench the intrinsic fluorescence of HSA through the formation of a KR-HSA complex in a static manner. In addition, the binding site is located in subdomain IIA as confirmed by competitive experiments using site-specific warfarin and ibuprofen, and the driving forces include hydrogen bonds, van der Waals forces and electrostatic interaction derived from a thermodynamic analysis. The formation of KR-HSA is exothermic and spontaneous. Although there is no hydrophobic interaction around Tyr and Trp residues, the secondary structure of HSA changes through the formation of the KR-HSA complex. In addition, docking results visualized and further supported these results. Finally, these results can provide more information to further investigate the use of KR on the prevention of diabetic complications.

SUBMITTER: Zhang W

PROVIDER: S-EPMC5450801 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature

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Insight into the binding interaction of kaempferol-7-O-α-L-rhamnopyranoside with human serum albumin by multiple fluorescence spectroscopy and molecular modeling.

Zhang Wenting W Chen Chun C Zhang Chunping C Duan Jingyu J Yao Huankai H Li Yan Y Meng Aiguo A Shi Jun J

Experimental and therapeutic medicine 20170504 6

Human serum albumin (HSA) is a transporting protein that has multiple functions. The binding interaction between HSA and small molecules affects its function and efficacy of small molecules. The present study reports that kaempferol-7-O-α-L-rhamnopyranoside (KR) interacts with HSA as indicated by multiple fluorescence spectroscopy and molecular modeling. KR can quench the intrinsic fluorescence of HSA through the formation of a KR-HSA complex in a static manner. In addition, the binding site is ...[more]

PMID: 28588690

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Project description:gamma-Aminobutyric acid (GABA) is a naturally occurring inhibitory neurotransmitter and some of its derivatives showed potential to act as neuroprotective agents. With the aim of developing potential leads for anti-Alzheimer's drugs, in this study we synthesized a novel GABA derivative, methyl 4-(4-((2-(tert-butoxy)-2-oxoethyl)(4-methoxyphenyl)amino)benzamido)butanoate by a unique method of Buchwald-Hartwig cross coupling synthesis; with some modification the yield was significant (97 %) and spectroscopic analysis confirmed that the compound was highly pure (98.8 % by HPLC). The druglikeness properties such as logP, logS, and polar surface area were 3.87, -4.86 and 94.17 Å(2) respectively and it satisfied the Lipinski's rule of five. We examined the binding behavior of the molecule to human serum albumin (HSA) and bovine serum albumin (BSA) which are known as universal drug carrier proteins. The molecule binds to the proteins with low micromolar efficiency and the calculated binding constants were 3.85 and 2.75 micromolar for BSA and HSA, respectively. Temperature dependent study using van't Hoff equation established that the binding was thermodynamically favorable and the changes in the Gibb's free energy, ?G for the binding process was negative. However, the binding of the molecule to HSA was enthalpy driven and the change of enthalpy (?H) was -10.63 kJ/mol, whereas, the binding to BSA was entropy driven and the change in entropy ?S was 222 J/mol. The molecular docking analysis showed that the binding sites of the molecule lie in the groove between domain I and domain III of BSA, whereas it is within the domain I in case of HSA, which also supported the different thermodynamic nature of binding with HSA and BSA. Molecular dynamics analysis suggested that the binding was stable with time and provided further details of the binding interaction. Molecular dynamics study also highlighted the effect of this ligand binding on the serum albumin structure.

Dataset Information

Insight into the binding interaction of kaempferol-7-O-?-L-rhamnopyranoside with human serum albumin by multiple fluorescence spectroscopy and molecular modeling.

Publications

Insight into the binding interaction of kaempferol-7-O-α-L-rhamnopyranoside with human serum albumin by multiple fluorescence spectroscopy and molecular modeling.

Similar Datasets

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