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- W2300846555 abstract "Introduction: The interaction of lomefloxacin (LMF) with human serum albumin (HSA) has been investigated by using fluorescence and circular dichroism spectroscopic for the first time. Participation of tyrosine and tryptophan groups in LMF-HSA complex is assessed using different excitation wavelengths. At 280 nm wavelength the tryptophanyl and tyrosyl residues in HSA are excited, whereas the 295 nm wavelength excites only tryptophanyl residues. Aim: The present study investigated the effects of LMF-HSA for determining the number of binding site, binding constant and the binding affinity of LMF and HSA. Materials and methods Fluorescence spectra were recorded the emission spectra of the free HSA and HAS-drag mixture were measured using the buffer solutions of drug in corresponding concentration as reference. Results: Fluorescence data revealed the number of binding sites, n, the binding constant values, K, and the binding affinity, Ksv, were noticed to be 1.5, 1.22 M and 1.64 M for LMF respectively. Conclusion: Interaction of HSA with LMF led to significant red shift of the protein fluorescence emission band (maximum 10 nm especially at high drug concentration, which indicated that the Amino acid residue Trp214 in the binding pocket has been brought to a more hydrophilic environment and the conformation of the protein has been changed. Circular dichroism spectra show a conformational change of the secondary structure of the protein leading to a loss in its helical content." @default.
- W2300846555 created "2016-06-24" @default.
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- W2300846555 date "2011-01-01" @default.
- W2300846555 modified "2023-09-26" @default.
- W2300846555 title "A SPECTROSCOPIC STUDY OF LOMEFLOXACIN BINDING TO HUMAN SERUM ALBUMIN" @default.
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