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H. Wang, H. Zou and Y. Zhang, “Multi-Site Binding of Fenoprofen to Human Serum Albumin Studied by a Combined Technique of Microdialysis with High Performance Liquid Chromatography,” Biomedical Chromatography, Vol. 12, No. 1, 1998, pp. 4-7. doi.org/10.1002/(SICI)1099-0801(199801/02)12:1<4::AID-BMC707>3.0.CO;2-K

has been cited by the following article:

• TITLE: Using of In-Situ Mercury Film Sensor Hyphenated with Affinity Voltammetry for High Throughput Drug-Protein Binding Studies

  AUTHORS: Ahmed K. Youssef, Deia Abd El-Hady

  KEYWORDS: Sensor; Affinity Voltammetry; Fenoprofen; Bovine Serum Albumin; Binding Constant

  JOURNAL NAME: American Journal of Analytical Chemistry, Vol.4 No.4, April 29, 2013

  ABSTRACT: A new simple and reliable in-situ mercury film sensor coupled with affinity differential pulse stripping voltammetry (ADSPV) or affinity cyclic voltammetry (ACV) was investigated. The interaction of fenoprofen with bovine serum albumin (BSA) onto the proposed electrochemical sensor was studied. The nature of the electrochemical process of fenoprofen by cyclic voltammetry was depicted. Reproducibility of the proposed method was checked giving a precision of 0.073 standard deviation. The limit of detection and limit of quantification were 7.0 and 22.0 nmol/L, respectively. Fenoprofen was interacted with BSA by 1:1 stoichiometry to form electroinactive supramolecular complex. The binding constant was precisely estimated by non-linear regression analysis based on the shifting of analyte peak potentials. The proposed experiments and data analysis could be used to investigate the drug-protein binding constant within a short analysis time compared to other chromatographic techniques.