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Electrochemical Studies of Camptothecin and Its Interaction with Human Serum Albumin

1
Department of Biochemistry and National Key Laboratory of Pharmaceutical Biotechnology, Nanjing University, Nanjing 210093, P. R. China
2
School of Life Science and Shanghai Key Laboratory of Bio-Energy Crops, Shanghai University, Shanghai 200444, P. R. China
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2007, 8(1), 42-50; https://doi.org/10.3390/i8010042
Received: 4 January 2007 / Accepted: 25 January 2007 / Published: 30 January 2007
(This article belongs to the Special Issue Interaction of Biological Molecules)
Camptothecin, an anticancer component from Camptotheca acuminate, mayinteract with human serum albumin (HSA) at the subdomain IIA (site I), and then convert toits inactive form(carboxylate form). In this paper, the detailed electrochemical behaviors ofcamptothecin at a pyrolytic graphite electrode is presented. The interaction betweencamptothecin and HSA is also studied by electrochemical technique. By comparing withbovine serum albumin (BSA), which is highly homologous to HSA, we prove thatcamptothecin can specifically bind to HSA. Meanwhile, the inhibitory influence of sodiumsalicylate to this binding is also discussed. View Full-Text
Keywords: Camptothecin; human serum albumin; cyclic voltammetry Camptothecin; human serum albumin; cyclic voltammetry
MDPI and ACS Style

Zhao, J.; Zheng, X.; Xing, W.; Huang, J.; Li, G. Electrochemical Studies of Camptothecin and Its Interaction with Human Serum Albumin. Int. J. Mol. Sci. 2007, 8, 42-50.

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