A mini-review of mass spectrometry using high-performance FTICR-MS methods

Heeren, Ron M. A.; Kleinnijenhuis, Anne J.; McDonnell, Liam A.; Mize, Todd H.

doi:10.1007/s00216-003-2446-4

Cited by 48 publications

(34 citation statements)

References 108 publications

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“…While the TOF/TOF experiments were useful in the identification of native Litset Pen4−1, advances in peptide fragmentation have been reported that hold promise for the intact analysis of penaeidins [64][65][66][67]. One of these technologies is electron capture dissociation (ECD) in conjunction with Fourier transform ion cyclotron resonance mass spectrometry (FTICR MS) [66,68,69].In an effort to further explore MS/MS approaches for fragmentation of intact penaeidins, FTICR MS in combination with ECD was used to generate fragments of the full-length Litset Pen3−4 without prior reduction of the disulfide bonds (Fig. 5).…”

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Diversity in penaeidin antimicrobial peptide form and function

Cuthbertson

Deterding

Williams

et al. 2008

Developmental & Comparative Immunology

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Penaeidins are a diverse family of two-domain antimicrobial peptides expressed in shrimp. Variation in penaeidin sequence results in functional diversity, which was discovered using synthetic reproductions of native penaeidins. An isoform of penaeidin class 3 from L. setiferus (Litset Pen3 −4) was synthesized using native ligation and compared directly with the synthetic penaeidin class 4 known to be expressed in the same organism. New antimicrobial activity data is included in this review that emphasizes differences in effectiveness that are apparent from a direct comparison of two classes. A novel approach to intact penaeidin analysis is presented in the form of Fourier Transform Ion-Cyclotron Resonance Mass Spectrometry, which has implications for the identification of individual penaeidin isoforms without chemical modification or enzymatic cleavage. The new information included in this review helps gather the perspective on relevance of penaeidin diversity to antimicrobial function, the use of synthetic peptides as tools to evaluate specific immune functions and the application of high mass resolution, top-down sequencing methods to the intact analysis of individual penaeidin isoforms. Publisher's Disclaimer: This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final citable form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. Keywords NIH Public Access Author ManuscriptDev Comp Immunol. Author manuscript; available in PMC 2009 January 1. Published in final edited form as:Dev Comp Immunol. 2008 ; 32(3): 167-181. NIH-PA Author ManuscriptNIH-PA Author Manuscript NIH-PA Author Manuscript OverviewAntimicrobial peptides (anti-MPs) are a diverse group of innate immune effector molecules that are utilized by multicellular organisms to prevent or combat infection by microbes. AntiMPs have been the subject of extensive review and several categories of anti-MPs have been described based on structural characteristics with certain themes being repeated throughout the living world [1][2][3][4]. Two prominent themes of anti-MP form that are relevant to this particular review include linear, proline-rich peptides, and cysteine-rich peptides that fold into a tertiary structure stabilized by disulfide bonds. These two separate themes provide a lead-in to the peptide family that is the primary focus of this review, the penaeidin family of anti-MPs.Many examples of short anti-MPs found in the literature contain a considerable percentage of Pro residues associated with other specific amino acids, particularly Arg, in repetitive motifs [5][6][7]. Such peptides have been well characterized in insects and mammals. Apidaecin, abaecin, drosocin, formaecin, pyrrhocoricin and lebo...

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Diversity in penaeidin antimicrobial peptide form and function

Cuthbertson

Deterding

Williams

et al. 2008

Developmental & Comparative Immunology

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“…MMA of these instruments is approximately 1 ppm, surpassing ion-traps by at least 2 orders of magnitude, and resolution can be routinely 100000. FTICR analysers are highly versatile and can be combined with both MALDI and ESI [20,21] ion sources. The extremely high mass resolution/MMA makes FTICR-MS the instrument of choice for studying protein isoforms [22] (and see below).…”

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confidence: 99%

Application of Mass Spectrometry in Proteomics

2005

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Mass spectrometry has arguably become the core technology in proteomics. The application of mass spectrometry based techniques for the qualitative and quantitative analysis of global proteome samples derived from complex mixtures has had a big impact in the understanding of cellular function. Here, we give a brief introduction to principles of mass spectrometry and instrumentation currently used in proteomics experiments. In addition, recent developments in the application of mass spectrometry in proteomics are summarised. Strategies allowing high-throughput identification of proteins from highly complex mixtures include accurate mass measurement of peptides derived from total proteome digests and multidimensional peptide separations coupled with mass spectrometry. Mass spectrometric analysis of intact proteins permits the characterisation of protein isoforms. Recent developments in stable isotope labelling techniques and chemical tagging allow the mass spectrometry based differential display and quantitation of proteins, and newly established affinity procedures enable the targeted characterisation of post-translationally modified proteins. Finally, advances in mass spectrometric imaging allow the gathering of specific information on the local molecular composition, relative abundance and spatial distribution of peptides and proteins in thin tissue sections.

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“…The principle underlying FTICR mass spectrometry forms the basis of its unique capabilities. There have been a couple of excellent reviews [25][26][27][28] that give very detailed descriptions of this technique, therefore only the very fundamentals are briefly described herein. FTMS uses the ICR principle to determine m/z values of ions, whereby ions are trapped in a cell that is located within a static magnetic field (Figure 1).…”

Section: Fourier Transform Ion Cyclotron Resonance (Fticr) Mass Spectmentioning

confidence: 99%

Investigation of Protein–Ligand Interactions by Mass Spectrometry

Sinz

2007

ChemMedChem

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The rate of drug discovery is greatly dependent on the development and improvement of rapid and reliable analytical methods that allow screening for protein-ligand interactions. The solution-based methods for investigating protein-ligand interactions by mass spectrometry (MS), which are discussed in this paper, are hydrogen/deuterium exchange of protein backbone amide hydrogens, and photoaffinity labeling. Moreover, MS analysis of intact noncovalent protein-ligand complexes is described. Fourier transform ion cyclotron resonance mass spectrometry (FTICR-MS) with its ultra-high resolution and excellent mass accuracy is also considered herein as it is gaining increasing popularity for a mass spectrometric investigation of protein-ligand interactions.

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A mini-review of mass spectrometry using high-performance FTICR-MS methods

Cited by 48 publications

References 108 publications

Diversity in penaeidin antimicrobial peptide form and function

Diversity in penaeidin antimicrobial peptide form and function

Application of Mass Spectrometry in Proteomics

Investigation of Protein–Ligand Interactions by Mass Spectrometry

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