Effect of albumin conformation on the binding of ciprofloxacin to human serum albumin: a novel approach directly assigning binding site.

@article{Ahmad2006EffectOA,
  title={Effect of albumin conformation on the binding of ciprofloxacin to human serum albumin: a novel approach directly assigning binding site.},
  author={Basir Ahmad and Suphiya Parveen and Rizwan Hasan Khan},
  journal={Biomacromolecules},
  year={2006},
  volume={7 4},
  pages={1350-6}
}
Human serum albumin (HSA) is known to exist as N (pH approximately 7), B (pH approximately 9), and F (pH approximately 3.5) isomeric forms and an equilibrium intermediate state (I) accumulate in the urea induced unfolding pathway of HSA around 4.8-5.2 M urea concentrations. These states displayed characteristic structure and functions. To elucidate the ciprofloxacin (CFX) binding behavior of HSA, the binding of ciprofloxacin with these conformational states of human serum albumin (HSA) has been… CONTINUE READING

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