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Analysis of binding interaction between pegylated puerarin and bovine serum albumin by spectroscopic methods and dynamic light scattering

From National Research Council Canada

DOIResolve DOI: https://doi.org/10.1016/j.saa.2011.08.065
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Affiliation
  1. National Research Council of Canada. NRC Plant Biotechnology Institute
FormatText, Article
SubjectBovine serum albumins; Dynamic light scattering (DLS); Fluorescence quenching; Pegylation; Puerarin; Binding sites; Body fluids; Circular dichroism spectroscopy; Dichroism; Dynamic light scattering; Fluorescence; Fluorescence spectroscopy; Glycols; Hydrophobicity; Motion Picture Experts Group standards; Organic compounds; Polyethylene glycols; Quenching; Refraction; Scattering; Spectroscopic analysis; Ultraviolet spectroscopy; Binding energy; bovine serum albumin; isoflavone derivative; macrogol derivative; puerarin; vasodilator agent; cattle; chemistry; circular dichroism; entropy; light; metabolism; protein binding; radiation scattering; spectrofluorometry; thermodynamics; ultraviolet spectrophotometry; Cattle; Circular Dichroism; Entropy; Isoflavones; Light; Polyethylene Glycols; Protein Binding; Scattering, Radiation; Serum Albumin, Bovine; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Thermodynamics; Vasodilator Agents
Abstract
The interaction between bovine serum albumin (BSA) and pegylated puerarin (Pur) in aqueous solution was investigated by UV-Vis spectroscopy, fluorescence spectroscopy and circular dichroism spectra (CD), as well as dynamic light scattering (DLS). The fluorescence of BSA was strongly quenched by the binding of pegylated Pur to BSA. The binding constants and the number of binding sites of mPEG 5000-Pur with BSA were 2.67 ± 0.12 and 1.37 ± 0.05 folds larger after pegylating, which were calculated from the data obtained from fluorescence quenching experiments. The enthalpy change (ΔH) and entropy change (ΔS) were calculated to be 4.09 kJ mol -1 and 20.01 J mol -1 K -1, respectively, according to Van't Hoff equation, indicating that the hydrophobic force plays a main role in the binding interaction between pegylated Pur and BSA. In addition, the negative sign for Gibbs free energy change (ΔG) implies that the interaction process is spontaneous. Moreover, the results of synchronous fluorescence and CD spectra demonstrated that the microenvironment and the secondary conformation of BSA were changed. Comparing with Pur, all our data collected indicated that pegylated Pur interacted with BSA in the same way as that of Pur, but docked into the hydrophobic pocket of BSA with more accessibility and stronger binding force. DLS measurements showed monomethoxy polyethylene glycol (mPEG) have an effect on BSA conformation, and revealed that changes in BSA size might be due to increases in binding constant and the absolute values of ΔG after Pur pegylation. © 2011 Elsevier B.V.
Publication date
In
  • Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy 83, no. 1 (2011): 453–460.
LanguageEnglish
Peer reviewedYes
NPARC number21271226
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Record identifier2eed927c-eb4d-4867-9360-f3c66ff64274
Record created2014-03-24
Record modified2020-04-21
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