Spectroscopic approach of the interaction study of Ceftriaxone and human serum albumin
Abu Teir, M. M.
Abu-Taha, M. I.
Darwish, S. M.
Abu-hadid, M. M
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 -helix than for the -sheets.
Ceftriaxone , amide I-III , binding mode , binding constant , protein secondary structure , Fourier transform IR , UV-spectroscopy , Flurosence spectroscopy