Chapter 14 - Identification of biologically active peptides by means of Fourier transform mass spectrometry

Abstract

Possessing the most various advantageous properties peptides are ubiquitous participants in nearly all biological processes. Elucidation of their structure is important in terms of physiology, for synthesis of their analogs, and for biomarkers discovery. New “omics” techniques and especially peptidomics, based on mass spectrometry (MS), have been applied to peptide structure elucidation. Fourier transform mass spectrometry (FTMS) offers advantages of high resolution and mass accuracy that are especially helpful in peptide mass fingerprinting and mass mapping. Tandem FTMS (a combination of FTMS with various ion activation and dissociation techniques) provides reliable information about the amino acid sequence. This chapter reviews application of FTMS for characterization and sequencing of bioactive peptides. Aspects of MS imaging, mass mapping, basics of different tandem MS methods, their advantages and drawbacks are discussed. Major peptidomics objects include amphibian skin secretion, venoms of vertebrates and invertebrates, neuropeptides of crustaceans and endogenous peptides in human biological fluids.