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

J Mol Recognit. Mar-Apr 1999;12(2):77-93. doi: 10.1002/(SICI)1099-1352(199903/04)12:2<77::AID-JMR448>3.0.CO;2-G.


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 (MALDI-TOF). 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. MALDI-TOF 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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antigen-Antibody Reactions
  • Binding, Competitive
  • Biosensing Techniques
  • Crotalid Venoms / chemistry
  • Crotalid Venoms / immunology
  • Humans
  • Immunoglobulin G / chemistry
  • Immunoglobulin G / immunology
  • Kinetics
  • Ligands
  • Mass Spectrometry / instrumentation
  • Mass Spectrometry / methods*
  • Molecular Sequence Data
  • Molecular Weight
  • Nucleic Acids / chemistry
  • Peptide Fragments / chemistry
  • Protein Binding
  • Proteins / chemistry*
  • Quality Control
  • Rabbits
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / instrumentation
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / methods
  • Subtraction Technique
  • Surface Plasmon Resonance / instrumentation
  • Surface Plasmon Resonance / methods*


  • Crotalid Venoms
  • Immunoglobulin G
  • Ligands
  • Nucleic Acids
  • Peptide Fragments
  • Proteins
  • myotoxin A