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× 10 3 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.
Transthyretin (TTR) aggregation has been characterized to be responsible for several amyloid diseases. Fourier transform infrared (FTIR) spectroscopy, �uorescence, and atomic force microscopy (AFM) are used to investigate secondary structure changes in transthyretin, induced upon thermal denaturation and interaction with pentobarbital. Spectral analysis revealed a strong static quenching of the intrinsic �uorescence of TTR by pentobarbital with a binding constant (�) estimated at 2.092 × 10 3 M −1 . Fourier self-deconvolution (FSD) technique is used to evaluates intensity changes in the spectra of the component bands in the amide I and amide II regions due to the changes in pentobarbital concentration in the protein complex. e increases of the relative intensities of the peaks at 1614 cm −1 and 1507 cm −1 are due to the increase of pentobarbital concentrations which is linked to the formation of oligomers in the protein.
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