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

✍ Scribed by Dobrin Nedelkov; Randall W. Nelson

• Publisher: John Wiley and Sons
• Year: 2000
• Tongue: English
• Weight: 177 KB
• Volume: 13
• Category: Article
• ISSN: 0952-3499
• DOI: 10.1002/1099-1352(200005/06)13:3<140::aid-jmr496>3.0.co;2-p

✦ Synopsis

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.