Differential interactions of camptothecin lactone and carboxylate forms with human blood components.

@article{Mi1994DifferentialIO,
  title={Differential interactions of camptothecin lactone and carboxylate forms with human blood components.},
  author={Zhenpeng Mi and Thomas G. Burke},
  journal={Biochemistry},
  year={1994},
  volume={33 34},
  pages={
          10325-36
        }
}
The intrinsic fluorescent emissions from the lactone and carboxylate forms of camptothecin have been exploited in order to elucidate their markedly different interactions with the various components of human blood. In phosphate-buffered saline (PBS) at pH 7.4, human serum albumin (HSA) preferentially binds the carboxylate form with a 150-fold higher affinity than the lactone form; these interactions result in camptothecin opening more rapidly and completely in the presence of HSA than in the… CONTINUE READING
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