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

D Nedelkov·R W Nelson
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Abstract

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.

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Biosensing TechniquesSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationJournal ArticleResearch Support, U.S. Gov't, P.H.S.Review

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D Nedelkov, R W Nelson. Practical considerations in BIA/MS: optimizing the biosensor-mass spectrometry interface.. https://doi.org/10.1002/1099-1352(200005%2F06)13%3A3%3C140%3A%3Aaid-jmr496%3E3.0.co%3B2-p

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