Biomolecular interaction analysis BIA

It is a feature of current developments in mass spectrometry that this method of analysis can be coupled or interfaced with other techniques. The interfacing may in fact be with further MS equipment (MS/MS), or with various separation techniques such as high-performance liquid chromatography (LC/MS), gas chromatography (GC/MS), electrophoresis, particularly high-resolution capillary electrophoresis (CE/ MS), and biomolecular interaction analysis (BIA/MS) (Krone 1997). 

Biomolecular interaction analysis (BIA) is a relatively new technique which enables the detection of biomolecules and the monitoring of interactions between two or more species to be carried out in real time, without the use of labels. The detection principle used depends on the phenomenon of Surface Plasmon Resonance (SPR). 

Biomolecular interaction analysis (BIA) based on siuTace plasmon resonance (SPR) is a popular affinity-based biosensor technology optimized for monitoring interactions between biomolecules in real time. BIA is an important analytical technique for the study of DNA-binding proteins and, therefore, the topic of a separate chapter of this book. This chapter discusses why and how BIA has been combined with MS, and the benefits and problems of this analytical union. 

Nelson RW, Krone JR. Advances in surface plasmon resonance biomolecular interaction analysis mass spectrometry (BIA/MS). J Mol Recognit 1999 12 77-93. 

Fig. 1 Biomolecular interaction analysis/mass spectrometry (BIA/MS). Biosensor chips are derivatized with affinant (or used with an affinant of streptavidin) and used in the BIA analysis of biological fluids. The chips are then introduced into a MALDI time-of-flight mass spectrometer and retained ligands analyzed by virtue of molecular weight.

Nelson, R.W. Krone, J.R. Advances in Surface Plasmon Resonance Biomolecular Interaction Analysis Mass Spectrometry (BIA/MS), J. Mol. Recognit. 12, 77-93 (1999). 

Krone, J.R., Nelson, R.W., Dogruel, D., Withams, P., Granzow, R., BIA/MS interfacing biomolecular interaction analysis with mass spectrometry, AnoZ. Biochem., 244,124—132, 1997. 

Biomolecular interaction analysis-mass spectrometry (BIA-MS), a combination of SPR with MS, was first explored by Krone et al. in 1996 where SPR was used to quantify interactions between proteins and MS was used to determine the structural features of die bound proteins. Review articles on SPR-MS describe recent progress in the field of SPR-MS, including future trends and possible applications. ... 

Appl Biochem Biotechnol Hypotheses Food Sci 71(5) 51-55 Nagata K, Handa H (2000) Real-time analysis of biomolecular interactions - applications of bia-core, 1st edn. Springer, Tokyo... 

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