Journal of
Biophysics and Structural Biology

  • Abbreviation: J. Biophys. Struct. Biol.
  • Language: English
  • ISSN: 2141-2200
  • DOI: 10.5897/JBSB
  • Start Year: 2009
  • Published Articles: 25

Full Length Research Paper

Spectroscopic approach of the interaction study of ceftriaxone and human serum albumin

Abu Teir M. M.*
  • Abu Teir M. M.*
  • Department of Physics, Faculty of Science, Al-Quds University, Jerusalem, Palestine.
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Ghithan J.
  • Ghithan J.
  • Department of Physics, Faculty of Science, Al-Quds University, Jerusalem, Palestine.
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Abu-Taha M. I.
  • Abu-Taha M. I.
  • Department of Physics, Faculty of Science, Al-Quds University, Jerusalem, Palestine.
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Darwish S. M.
  • Darwish S. M.
  • Department of Physics, Faculty of Science, Al-Quds University, Jerusalem, Palestine.
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Abu-hadid M. M
  • Abu-hadid M. M
  • Department of Immunology, Faculty of Medicine, Al-Quds University, Jerusalem, Palestine.
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  •  Received: 13 September 2013
  •  Accepted: 18 November 2013
  •  Published: 28 February 2014

Abstract

Under physiological conditions, interaction between ceftriaxone and human serum albumin was investigated by using fluorescence spectroscopy and ultra violet (UV) absorption spectrum. From spectral analysis, ceftriaxone showed a strong ability to quench the intrinsic fluorescence of human serum albumin (HSA) through a static quenching procedure. The binding constant (k) is estimated as K=1.02× 103 M-1 at 298 K. Fourier transform infrared spectroscopy (FT-IR) spectroscopy with Fourier self-deconvolution technique was used to determine the protein secondary structure and drug binding mechanisms. The observed spectral changes indicated the formation of H-bonding between ceftriaxone and HSA molecules at higher percentage for a-helix than for the b-sheets.

Key words: Ceftriaxone, amide I-III, binding mode, binding constant, protein secondary structure, Fourier transform IR, UV-spectroscopy, Flurosence spectroscopy.

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This article is published under the terms of the Creative Commons Attribution License 4.0

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