BIA/MS: Interfacing biomolecular interaction analysis with mass spectrometry

Jennifer R. Krone, Randall W. Nelson, David Dogruel, Peter Williams, Russ Granzow

Research output: Contribution to journalArticle

136 Scopus citations

Abstract

Biomolecular interaction analysis (BIA) which utilizes surface plasmon resonance (SPR) detection of affinity-captured analytes has been interfaced with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI). Femtomole quantities of a peptide, myotoxin a, were detected by direct MALDI analysis of sensor chips used during BIA of a polyclonal anti-myotoxin a IgG/myotoxin a system. Further, different interactive surfaces (flow cells) present on a single biosensor were targeted individually for mass spectrometric analysis. System compatibility of the combined approach was demonstrated with sensitivities, detection limits, and analytical performances comparable to those intrinsic to the individual analyses. The combined approach unites the real-time capabilities of SPR- based BIA with the qualitative specificity of mass spectrometry.

Original languageEnglish (US)
Pages (from-to)124-132
Number of pages9
JournalAnalytical Biochemistry
Volume244
Issue number1
DOIs
StatePublished - Jan 1 1997

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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