Practical considerations in BIA/MS: Optimizing the biosensor-mass spectrometry interface

Dobrin Nedelkov, Randall W. Nelson

Research output: Contribution to journalArticlepeer-review

68 Scopus citations


Biomolecular interaction analysis mass spectrometry (BIA/MS) is a multiplexed analytical technique that utilizes a unique combination of surface plasmon resonance (SPR) and matrix assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) for the detection and analysis of small amounts of proteins residing in complex biological systems. In order to achieve high sensitivity during BIA/MS, certain experimental parameters and sequences of events need to be optimized and maintained. Immobilized ligand density, flow rate and biosensor control (in SPR-BIA) and matrix choice and application (in MALDI-TOF MS) have significant influence on the final outcome of the BIA/MS analysis and, consequently, need to be optimized and carefully controlled. In addition, chip washing and cutting are essential in converting the SPR-active sensor chips into target surfaces amenable to MALDI-TOF MS. Reviewed here are the prerequisites for successfully interfacing SPR-BIA with MALDI-TOF MS. Copyright (C) 2000 John Wiley and Sons, Ltd.

Original languageEnglish (US)
Pages (from-to)140-145
Number of pages6
JournalJournal of Molecular Recognition
Issue number3
StatePublished - May 2000


  • BIA/MS
  • Biosensor
  • Chip
  • MALDI-TOF mass spectrometry

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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