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Interaction of a Model Hydrophobic Drug Dimethylcurcumin with Albumin Nanoparticles

  • R. P. Das
  • B. G. SinghEmail author
  • A. KunwarEmail author
  • K. I. Priyadarsini
Article
  • 16 Downloads

Abstract

The aim of present study was to investigate the binding interactions of a model hydrophobic molecule, dimethylcurcumin (DMC) with nanoparticle form of bovine serum albumin (BSA) using fluorescence spectroscopy techniques. For this, BSA nanoparticles (size = 62.0 ± 3.5 nm, molecular weight = 11,243 ± 3445 kD) prepared by thermal denaturation method was mixed with DMC in solution and monitored for fluorescence emission of tryptophan (Trp) residue as well as DMC separately. The emission maximum of DMC in nanoparticles form exhibited more blue sift and quenched the excited state of tryptophan (Trp) by six fold higher than in the native form of BSA. By analyzing Trp fluorescence, the mean binding constant (K) estimated for the interaction of DMC with native and nanoparticles forms of BSA was 2.7 ± 0.4 × 104 M−1 and 1.5 ± 0.5 × 105 M−1 respectively. Together these results suggested that DMC experienced a more rigid environment in nanoparticles than in native form of BSA. Additionally the above determined K values were in agreement with those reported previously by absorption techniques. Further direct energy transfer was observed between Trp and DMC, using which the distance (r) calculated between them was 28.25 ± 0.27 Ǻ in BSA native. Similar analysis involving BSA nanoparticle and DMC revealed a distance of 24.25 ± 1.05 Ǻ between the hydrophobic core and the ligand. Finally interaction of DMC with BSA was validated through molecular docking studies, which indicated sub-domain IIA as the binding site of DMC. Thus it is concluded that intrinsic fluorescence of protein can be utilized to study the interaction of its different physical forms with any hydrophobic ligand.

Keywords

Albumin Nanoparticles Fluorescence spectroscopy Binding constant Fluorescence energy transfer 

Notes

Funding

N/A.

Compliance with Ethical Standards

Conflict of interest

The authors declare that they have no conflict of interest.

Informed Consent

N/A.

Research Involving Human Participants or Animals

This article does not contain any studies with human participants or animals performed by any of the authors.

Supplementary material

10930_2019_9866_MOESM1_ESM.docx (1.2 mb)
Supplementary material 1 (DOCX 1233 kb)

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Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2019

Authors and Affiliations

  1. 1.Radiation & Photochemistry DivisionBhabha Atomic Research CentreMumbaiIndia
  2. 2.Homi Bhabha National InstituteMumbaiIndia
  3. 3.Chemistry DivisionBhabha Atomic Research CentreMumbaiIndia

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