Comparative Analysis of KP-HSA Complex by Spectroscopic Methods

• Authors: M. Mąciażek-Jurczyk , J. Równicka-Zubik , R. Dyja , A. Sułkowska
• Languages of publication: EN

Abstracts

EN

The main objective of the presented study was to characterize the high (HAS) and low affinity (LAS) binding sites of ketoprofen (KP) in human serum albumin (HSA) structure with the use of spectrofluorescence and proton nuclear magnetic resonance spectroscopy. In vitro fluorescence analysis was used to estimate the effect of KP on the HSA fluorescence. The association constants K_{a} [M^{-1}] of KP-HSA complex in the HAS were determined with the use of Scatchard, Klotz, and Hill analysis. The quenching K_{Q} [M^{-1}] constants were determined on the basis of the Stern-Volmer equation. Binding of ketoprofen to plasma protein was also studied with the use of 8-anilinonapthalene-1-sulfonic acid (ANS) and 5-dimethylaminonaphthalene-1-sulfonic acid (DNSA) as the fluorescence probes in IIIA and IIA subdomains of HSA, respectively. To estimate the cooperativeness in proteins Hill's coefficient n_{H} was used. The analysis of proton nuclear magnetic resonance spectra of KP in the presence of HSA allows us to observe the interactions between aromatic rings of the drug and the rings of amino acids located in the hydrophobic subdomains of the protein on the basis of the changes of chemical shifts Δ σ [ppm] of drug protons resonances. Moreover the K_{a} constants [M^{-1}] of KP-HSA complex in the LAS were determined.

Keywords

EN

33.50.-j; 33.50.Dq; 82.56.-b; 87.14.-g; 87.14.E-

Discipline

• 87.14.-g: Biomolecules: types
• 33.50.-j: Fluorescence and phosphorescence; radiationless transitions, quenching (intersystem crossing, internal conversion)(for energy transfer, see also section 34; for biophysical applications, see 87.64.kv)
• 87.14.E-: Proteins
• 82.56.-b: Nuclear magnetic resonance(see also 33.25.+k Nuclear resonance and relaxation in atomic and molecular physics; 76.60.-k Nuclear magnetic resonance and relaxation; 76.70.-r Magnetic double resonances and cross effects in condensed matter)
• 33.50.Dq: Fluorescence and phosphorescence spectra

• Publisher: Institute of Physics, Polish Academy of Sciences
• Journal: Acta Physica Polonica A
• Year: 2013
• Volume: 123
• Issue: 4
• Pages: 673-680

Dates

published

2013-04

received

2012-08-09

(unknown)

2013-02-02

Contributors

author

M. Mąciażek-Jurczyk

• Department of Physical Pharmacy, Medical University of Silesia, Jagiellońska 4, 41-200 Sosnowiec, Poland

author

J. Równicka-Zubik

• Department of Physical Pharmacy, Medical University of Silesia, Jagiellońska 4, 41-200 Sosnowiec, Poland

author

R. Dyja

• Department of Physical Pharmacy, Medical University of Silesia, Jagiellońska 4, 41-200 Sosnowiec, Poland

author

A. Sułkowska

• Department of Physical Pharmacy, Medical University of Silesia, Jagiellońska 4, 41-200 Sosnowiec, Poland

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Identifiers

DOI

10.12693/APhysPolA.123.673