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BIA/MS: Interfacing Biomolecular Interaction Analysis with Mass Spectrometry

✍ Scribed by Jennifer R. Krone; Randall W. Nelson; David Dogruel; Peter Williams; Russ Granzow

Publisher
Elsevier Science
Year
1997
Tongue
English
Weight
161 KB
Volume
244
Category
Article
ISSN
0003-2697

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✦ Synopsis

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.

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