Mass spectrometry is a powerful analytical technique that is used to identify unknown compounds, to quantify known materials, and to elucidate the structural and chemical properties of molecules. In analyzing the effects of experimental drugs on the brain, it is the sole technique for identifying the presence and structure of neuropeptides--substances that indicate the effect of the drug. Mass Spectrometry and Hyphenated Techniques in Neuropeptide Research specifically explains how to apply the technology to this process. Because the book is written by mass spectrometry users, as opposed to mass spectrometrists, the focus remains on practical applications of the technique. The authors demonstrate how mass spectrometry works, how to apply the technique to research, which types of instrumentation should be used for particular requirements, and how to plan experiments. Readers will learn why mass spectrometry provides more outcome features than other techniques in neuropeptide analysis, including simultaneous detection, identification of substances present in mixtures, and sequence information even when the residues are modified, blocked, or unusual. Among the chapters in this comprehensive text are: -Sequencing of Peptides by Nanospray Mass Spectrometry -Laser-Machined Microdevices for Mass Spectrometry -Electron Capture Dissociation of Peptides -Synthesis of Combinatorial Peptide Libraries -Analysis of Tissues That Reflect Nervous System Disease Doctoral students, researchers, and industry professionals in pharmacology, chemistry, biochemistry/biotechnology, and medicine will find Mass Spectrometry and Hyphenated

Table of Contents:
Preface. Contributors. PART 1: INTRODUCTION AND GENERAL DESCRIPTION. Introduction: Mass Spectrometry of Peptides and Proteins: A Personal Historical Viear (P. Roepstorff).Neuropeptides in CNS Tissue and Body Fluids: Functional Aspects and Strategies for Their Identification, Purification, and Characterization (F. Nyberg). Mass Spectrometry Instrumentation (A. Brinkmalm and G. Brickmalm). PART 2: HYPHENATED TECHNIQUES. Capillary and Nano LC Coupled with Mass Spectrometry (M. Raida). Capillary Electrophoresis Coupled to Mass Spectrometry for Peptide and Protein Analysis (M. Wetterhall, et al.).Sequencing of Neuroeptides by Nanoelectrospray Mass Spectrometry (J. Kast & M. Wilm). Laser Machined Microdevices for Mass Spectrometry (Y. Lin, et al.).Endogeneous Release and Metabolism of Neuropeptides Utilizing in vivo Microdialysis Microelectrospray Mass Spectrometry (P. Andren, et al.). Biomolecular Interaction Analysis Mass Spectrometry (BIA/MS) (D. Nedelkov & R. Nelson). Ultrasensitive MALDI TOF MS with Picoliter Volume Sample Handling (D. Ericsson & J. Bergquist). PART 3: SELECTED APPLICATIONS IN PEPTIDE RESEARCH. Peptide Mapping Using MALDI TOF MS (U. Hellman). Electron Capture Dissociation of Peptides (R. Zubarev). Synthesis of Combinatorial Peptide Libraries (K. Rolka). Fourier Transform Ion Cyclotron Resonance Mass Spectrometry for Peptide Analysis (K Hakansson, et al.). Peptide Sequencing Promoted by N Terminal Derivatization (D. Barofsky and T. Chen). MALDI TOF/TOF Technology for Peptide Sequencing and Protein Identification (P. Juhasz, et al.). Quantitative Analysis of Neuropeptides by MALDI TOF MS(J. Gobom & E. Nordhoff). PART 4: SELECTED APPLICATIONS IN BIOSCIENCES. Characterization of Peptides Bound to the Rat Class I MHC Molecule RTI AIc1 (R. Jones, et al.).Analysis of Neuropeptides in Cerebrospinal Fluid and Neural and Neuroendocrine Tissues by MALDI TOFMS (C. Nilsson). Neuropeptides Processing (P. Suder, et al.).Measuring Neuropeptides with Single Cell MALDI MS (L. Li and J. Sweedler). Dynamics of Cell Nucleus/Lymphocyte Nuclei Associated Peptides Studied by Mass Spectrometry and Future Peptidomic Aspects (J. Berquist and R. Ekman). Appendix (A. Sciubisz). Index.