Biomolecular Interaction Analysis Mass Spectrometry

Dobrin Nedelkov, Randall W. Nelson

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

Biomolecular interaction analysis mass spectrometry (BIA/MS) is a multidimensional methodology for functional and structural protein analysis. Proteins are affinity captured and quantified from a solution via ligands covalently attached on the SPR sensor surface. Because the SPR detection is nondestructive, proteins retrieved on the SPR sensing surface can be further analyzed via mass spectrometry, either directly from the sensor/chip surface or separately, following elution and microrecovery. Detection of attomole amounts of proteins from complex biological mixtures is possible via the combined SPR-MS approach. A chip cutter with a circular heated cutter head is used for excising a chip or plastic mount of a defined circular shape that fits into an appropriately configured MALDI mass spectrometer target. The MALDI matrix is applied to the chip via an aerosol-spraying device. MALDI-TOF mass spectrometry analysis from the chip surface is performed on a custom-made MALDITOF mass spectrometer. The instrument consists of a linear translation stage or ion source capable of precise targeting of each of the flow cells under a focused laser spot. © 2006

Original languageEnglish (US)
Title of host publicationCell Biology, Four-Volume Set
PublisherElsevier Inc.
Pages279-284
Number of pages6
Volume4
ISBN (Print)9780121647308
DOIs
StatePublished - Dec 1 2006

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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