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.This work was supported by the German Research Foundation DFG Grant No. DR228/24-2
