Premium
Practical considerations in BIA/MS: optimizing the biosensor–mass spectrometry interface
Author(s) -
Nedelkov Dobrin,
Nelson Randall W.
Publication year - 2000
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/1099-1352(200005/06)13:3<140::aid-jmr496>3.0.co;2-p
Subject(s) - mass spectrometry , surface plasmon resonance , interfacing , biosensor , chemistry , matrix assisted laser desorption/ionization , chromatography , analytical chemistry (journal) , matrix (chemical analysis) , desorption , nanotechnology , materials science , computer science , nanoparticle , computer hardware , adsorption , biochemistry , organic chemistry
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 © 2000 John Wiley & Sons, Ltd.