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

@article{citeulike:5903777, 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. Copyright {\copyright} 2000 John Wiley \& Sons, Ltd.}, address = {Intrinsic Bioprobes Inc., 2009 E. 5th Street, Suhe 11, Tempe, AZ 85281, USA}, author = {Nedelkov, Dobrin and Nelson, Randall W.}, citeulike-article-id = {5903777}, citeulike-linkout-0 = {http://dx.doi.org/10.1002/1099-1352(200005/06)13:3%3C140::AID-JMR496%3E3.0.CO;2-P}, citeulike-linkout-1 = {http://www3.interscience.wiley.com/cgi-bin/abstract/72508078/ABSTRACT}, doi = {10.1002/1099-1352(200005/06)13:3%3C140::AID-JMR496%3E3.0.CO;2-P}, issn = {1099-1352}, journal = {Journal of Molecular Recognition}, keywords = {biacore, id-qd, mass-spectrometry, pa, spr}, number = {3}, pages = {140--145}, posted-at = {2009-10-06 22:14:47}, priority = {2}, title = {Practical considerations in BIA/MS: optimizing the biosensor-mass spectrometry interface}, url = {http://dx.doi.org/10.1002/1099-1352(200005/06)13:3%3C140::AID-JMR496%3E3.0.CO;2-P}, volume = {13}, year = {2000} }

TY - JOUR ID - citeulike:5903777 L3 - citeulike-article-id:5903777 N2 - 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. IS - 3 JF - Journal of Molecular Recognition SN - 1099-1352 AD - Intrinsic Bioprobes Inc., 2009 E. 5th Street, Suhe 11, Tempe, AZ 85281, USA EP - 145 TI - Practical considerations in BIA/MS: optimizing the biosensor-mass spectrometry interface VL - 13 SP - 140 KW - biacore KW - id-qd KW - mass-spectrometry KW - pa KW - spr AU - Nedelkov, Dobrin AU - Nelson, Randall PY - 2000/// UR - http://dx.doi.org/10.1002/1099-1352(200005/06)13:3%3C140::AID-JMR496%3E3.0.CO;2-P ER -