A study of the interactions between carboplatin and blood plasma proteins using size exclusion chromatography coupled to inductively coupled plasma mass spectrometry

Ruimin Xie, Willie Johnson, Lorna Rodriguez, Murugesan Gounder, Gene S. Hall, Brian Buckley

Research output: Contribution to journalArticlepeer-review

50 Scopus citations

Abstract

To study the carboplatin-protein interaction, a sensitive method using size exclusion chromatography coupled to inductively coupled plasma mass spectrometry (SEC-ICP-MS) was developed. The complexes formed between plasma proteins and carboplatin were monitored and identified with this method. Composite blood plasma samples from patients who were undergoing chemotherapy were analyzed, and carboplatin was found to bind plasma proteins. In addition, blank plasma samples were spiked with carboplatin and were analyzed as a time course study, and the results confirmed that carboplatin formed complexes with plasma proteins, primarily albumin and γ-globulin. To further substantiate the study, these two proteins were incubated with carboplatin. The binding between carboplatin and these proteins was then characterized qualitatively and quantitatively. In addition to a one-to-one binding of Pt to protein, protein aggregation was observed. The kinetics of the binding process of carboplatin to albumin and γ-globulin was also studied. The initial reaction rate constant of carboplatin binding to albumin was determined to be 0.74M -1min-1, while that for γ-globulin was 1.01M -1min-1, which are both lower than the rate constant of the cisplatin-albumin reaction previously reported.

Original languageEnglish (US)
Pages (from-to)2815-2822
Number of pages8
JournalAnalytical and Bioanalytical Chemistry
Volume387
Issue number8
DOIs
StatePublished - Apr 2007

All Science Journal Classification (ASJC) codes

  • Analytical Chemistry
  • Biochemistry

Keywords

  • Carboplatin
  • Metal speciation
  • Protein complexation
  • SEC-ICP-MS

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