Blog
About

6
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: not found

      Molecular interaction of 2,4-diacetylphloroglucinol (DAPG) with human serum albumin (HSA): The spectroscopic, calorimetric and computational investigation.

      Read this article at

      ScienceOpenPublisherPubMed
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Drug molecule interaction with human serum albumin (HSA) affects the distribution and elimination of the drug. The compound, 2,4-diacetylphloroglucinol (DAPG) has been known for its antimicrobial, antiviral, antihelminthic and anticancer properties. However, its interaction with HSA is not yet reported. In this study, the interaction between HSA and DAPG was investigated through steady-state fluorescence, time-resolved fluorescence (TRF), circular dichroism (CD), Fourier transform infrared (FT-IR) spectroscopy, isothermal titration calorimetry (ITC), molecular docking and molecular dynamics simulation (MDS). Fluorescence spectroscopy results showed the strong quenching of intrinsic fluorescence of HSA due to interaction with DAPG, through dynamic quenching mechanism. The compound bound to HSA with reversible and moderate affinity which explained its easy diffusion from circulatory system to target tissue. The thermodynamic parameters from fluorescence spectroscopic data clearly revealed the contribution of hydrophobic forces but, the role of hydrogen bonds was not negligible according to the ITC studies. The interaction was exothermic and spontaneous in nature. Binding with DAPG reduced the helical content of protein suggesting the unfolding of HSA. Site marker fluorescence experiments revealed the change in binding constant of DAPG in the presence of site I (warfarin) but not site II marker (ibuprofen) which confirmed that the DAPG bound to site I. ITC experiments also supported this as site I marker could not bind to HSA-DAPG complex while site II marker was accommodated in the complex. In silico studies further showed the lowest binding affinity and more stability of DAPG in site I than in site II. Thus the data presented in this study confirms the binding of DAPG to the site I of HSA which may help in further understanding of pharmacokinetic properties of DAPG.

          Related collections

          Author and article information

          Journal
          Spectrochim Acta A Mol Biomol Spectrosc
          Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy
          Elsevier BV
          1873-3557
          1386-1425
          Aug 05 2017
          : 183
          Affiliations
          [1 ] Centre for Bioinformatics, Pondicherry University, Pondicherry, India.
          [2 ] Department of Biotechnology, Pondicherry University, Pondicherry, India.
          [3 ] Centre for Bioinformatics, Pondicherry University, Pondicherry, India. Electronic address: krishna.bic@pondiuni.edu.in.
          [4 ] Department of Biotechnology, Pondicherry University, Pondicherry, India. Electronic address: sakthivel.dbt@pondiuni.edu.in.
          Article
          S1386-1425(17)30280-9
          10.1016/j.saa.2017.04.012
          28441541

          Comments

          Comment on this article