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Spectroscopic approach of the interaction study of ceftriaxone and human serum albumin
Author(s) -
Teir M. M. Abu,
Jafar Ghithan,
M. I. Abu-Taha,
S. Darwish,
Mahmoud M. Abu-hadid
Publication year - 2014
Publication title -
journal of biophysics and structural biology
Language(s) - English
Resource type - Journals
ISSN - 2141-2200
DOI - 10.5897/jbsb2013.0045
Subject(s) - chemistry , human serum albumin , fourier transform infrared spectroscopy , spectroscopy , binding constant , protein secondary structure , fluorescence spectroscopy , ceftriaxone , infrared spectroscopy , analytical chemistry (journal) , quenching (fluorescence) , absorption spectroscopy , fluorescence , binding site , chromatography , biochemistry , organic chemistry , antibiotics , optics , physics , quantum mechanics
-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 -helix than for the -sheets.

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