Advances in surface plasmon resonance biomolecular interaction analysis mass spectrometry (BIA/MS)

Randall W. Nelson, Jennifer R. Krone

Research output: Contribution to journalReview articlepeer-review

70 Scopus citations


Ongoing, worldwide efforts in genomic and protein sequencing, and the ability to readily access corresponding sequence databases, have emphatically driven the development of high-performance bioanalytical instrumentation capable of characterizing proteins and protein-ligand interactions with great accuracy, speed and sensitivity. Two such analytical techniques have arisen over the past decade to play key roles in the characterization of proteins: surface plasmon resonance biomolecular interaction analysis (SPR-BIA) and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDITOF). SPR-BIA is used in the real-time investigation of biomolecular recognition events, and is thereby capable of providing details on the association and dissociation kinetics involved in the interaction, information ultimately leading to the determination of dissociation constants involved in the event. MALDITOF is used in the structural characterization, identification and sensitive detection of biomolecules. Although the two techniques have found many independent uses in bioanalytical chemistry, the combination of the two, to form biomolecular interaction analysis mass spectrometry (BIA/MS), enables a technique of analytical capabilities greater than those of the component parts. Reviewed here are issues of concern critical to maintaining high-levels of performance throughout the multiplexed analysis, as well as examples illustrating the potential analytical capabilities of BIA/MS.

Original languageEnglish (US)
Pages (from-to)77-93
Number of pages17
JournalJournal of Molecular Recognition
Issue number2
StatePublished - Mar 1999


  • Affinity interaction
  • BIA
  • Protein identification
  • Proteomics
  • Quantitation

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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