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Volumn 21, Issue 1, 2010, Pages 104-111

N-Terminal Tagging Strategy for De Novo Sequencing of Short Peptides by ESI-MS/MS and MALDI-MS/MS

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; AMINO GROUP; AMINO MOIETY; AUTOMATIC ALGORITHMS; DE NOVO SEQUENCING; EDMAN DEGRADATION; ESI-MS/MS; FT-ICR MS; ION SERIES; LYSINE SIDE CHAINS; MALDI MS/MS; MALDI-TOF/TOF; N-TERMINALS; TETRAFLUOROBORATES; TOF SPECTRUM;

EID: 73449086295     PISSN: 10440305     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jasms.2009.09.008     Document Type: Article
Times cited : (38)

References (48)
  • 1
    • 0032444189 scopus 로고    scopus 로고
    • Antimicrobial Peptides from Amphibian Skin: What Do They Tell Us?
    • Simmaco M., Mignogna G., and Barra D. Antimicrobial Peptides from Amphibian Skin: What Do They Tell Us?. Biopolymers 47 6 (1998) 435-450
    • (1998) Biopolymers , vol.47 , Issue.6 , pp. 435-450
    • Simmaco, M.1    Mignogna, G.2    Barra, D.3
  • 2
    • 33746131996 scopus 로고    scopus 로고
    • Host-Defense Peptide Profiles of the Skin Secretions of Interspecific Hybrid Tree Frogs and Their Parents, Female Litoria splendida and male Litoria caerulea
    • Pukala T.L., Bertozzi T., Donnellan S.C., Bowie J.H., Surinya-Johnson K.H., Liu Y., Jackway R.J., Doyle J.R., Llewellyn L.E., and Tyler M.J. Host-Defense Peptide Profiles of the Skin Secretions of Interspecific Hybrid Tree Frogs and Their Parents, Female Litoria splendida and male Litoria caerulea. FEBS J 273 15 (2006) 3511-3519
    • (2006) FEBS J , vol.273 , Issue.15 , pp. 3511-3519
    • Pukala, T.L.1    Bertozzi, T.2    Donnellan, S.C.3    Bowie, J.H.4    Surinya-Johnson, K.H.5    Liu, Y.6    Jackway, R.J.7    Doyle, J.R.8    Llewellyn, L.E.9    Tyler, M.J.10
  • 3
    • 0028707742 scopus 로고
    • Biosynthesis of Defensins and Other Antimicrobial Peptides
    • Marsh J., and Goode J.A. (Eds), John Wiley & Sons, Chichester, UK
    • Tomas G. Biosynthesis of Defensins and Other Antimicrobial Peptides. In: Marsh J., and Goode J.A. (Eds). Ciba Foundation Symposium 186-Antimicrobial Peptides (1994), John Wiley & Sons, Chichester, UK 62-76
    • (1994) Ciba Foundation Symposium 186-Antimicrobial Peptides , pp. 62-76
    • Tomas, G.1
  • 4
    • 0000952847 scopus 로고
    • Bioactive Secretions of the Amphibian Integument
    • Heatwole H., Barthalmus G.T., and Heatwole A.Y. (Eds), Surrey Beatty and Sons, Chipping Norton
    • Erspamer V. Bioactive Secretions of the Amphibian Integument. In: Heatwole H., Barthalmus G.T., and Heatwole A.Y. (Eds). Amphibian Biology Vol. I (1994), Surrey Beatty and Sons, Chipping Norton 178-350
    • (1994) Amphibian Biology , vol.I , pp. 178-350
    • Erspamer, V.1
  • 6
    • 67049154413 scopus 로고    scopus 로고
    • Bioactive Peptides from Ranid Frog Skin Secretions: Modern Approach to Mass Spectrometric de novo Sequencing
    • Samgina T.Y., Artemenko K.A., Gorshkov V.A., and Lebedev A.T. Bioactive Peptides from Ranid Frog Skin Secretions: Modern Approach to Mass Spectrometric de novo Sequencing. Russ. Chem. Bull. 57 5 (2008) 1061-1072
    • (2008) Russ. Chem. Bull. , vol.57 , Issue.5 , pp. 1061-1072
    • Samgina, T.Y.1    Artemenko, K.A.2    Gorshkov, V.A.3    Lebedev, A.T.4
  • 9
    • 41049089032 scopus 로고    scopus 로고
    • Oxidation Versus Carboxyamidomethylation of S-S Bond in Ranid frog peptides: Pro and Contra for De Novo MALDI-MS Sequencing
    • Samgina T.Y., Artemenko K.A., Gorshkov V.A., Poljakov N.B., and Lebedev A.T. Oxidation Versus Carboxyamidomethylation of S-S Bond in Ranid frog peptides: Pro and Contra for De Novo MALDI-MS Sequencing. J. Am. Soc. Mass Spectrom. 19 4 (2008) 479-487
    • (2008) J. Am. Soc. Mass Spectrom. , vol.19 , Issue.4 , pp. 479-487
    • Samgina, T.Y.1    Artemenko, K.A.2    Gorshkov, V.A.3    Poljakov, N.B.4    Lebedev, A.T.5
  • 11
    • 0021952988 scopus 로고
    • Tryptophyllins from Extracts of Phyllomedusa rhodei Skin: New Tetra-, Penta- and Heptapeptides. Further Studies
    • Gozzini L., Montecucchi P., Erspamer V., and Melchiorri P. Tryptophyllins from Extracts of Phyllomedusa rhodei Skin: New Tetra-, Penta- and Heptapeptides. Further Studies. Int. J. Pept. Prot. Res. 25 3 (1985) 323-329
    • (1985) Int. J. Pept. Prot. Res. , vol.25 , Issue.3 , pp. 323-329
    • Gozzini, L.1    Montecucchi, P.2    Erspamer, V.3    Melchiorri, P.4
  • 12
    • 0021470989 scopus 로고
    • Syntheses of Tetra- and Pentapeptides from Skin Extracts of Phyllomedusa rhodei (tryptophyllins)
    • Perseo G., and De Castiglione R. Syntheses of Tetra- and Pentapeptides from Skin Extracts of Phyllomedusa rhodei (tryptophyllins). Int J Pept Protein Res. 24 2 (1984) 155-160
    • (1984) Int J Pept Protein Res. , vol.24 , Issue.2 , pp. 155-160
    • Perseo, G.1    De Castiglione, R.2
  • 13
    • 0000322776 scopus 로고    scopus 로고
    • The Structures of New Peptides From the Australian Red Tree Frog Litoria rubella. The Skin Peptide Profile as a Probe for the Study of Evolutionary Trends of Amphibians
    • Steinborner S.T., Wabnitz P.A., Waugh R.J., Bowie J.H., Gao C.W., Tyler M.J., and Wallace J.C. The Structures of New Peptides From the Australian Red Tree Frog Litoria rubella. The Skin Peptide Profile as a Probe for the Study of Evolutionary Trends of Amphibians. Aust. J. Chem. 49 9 (1996) 955-963
    • (1996) Aust. J. Chem. , vol.49 , Issue.9 , pp. 955-963
    • Steinborner, S.T.1    Wabnitz, P.A.2    Waugh, R.J.3    Bowie, J.H.4    Gao, C.W.5    Tyler, M.J.6    Wallace, J.C.7
  • 15
    • 4143117846 scopus 로고    scopus 로고
    • Peptides from the Skin Glands of the Australian Buzzing Tree Frog Litoria electrica. Comparison with the Skin Peptides of the Red Tree Frog Litoria rubella
    • Wabnitz P.A., Bowie J.H., Wallace J.C., and Tyler M.J. Peptides from the Skin Glands of the Australian Buzzing Tree Frog Litoria electrica. Comparison with the Skin Peptides of the Red Tree Frog Litoria rubella. Aust. J. Chem. 52 7 (1999) 639-646
    • (1999) Aust. J. Chem. , vol.52 , Issue.7 , pp. 639-646
    • Wabnitz, P.A.1    Bowie, J.H.2    Wallace, J.C.3    Tyler, M.J.4
  • 16
    • 0346995402 scopus 로고    scopus 로고
    • Pachymedusa dacnicolor Tryptophyllin-1: Structural Characterization, Pharmacological Activity, and Cloning of Precursor cDNA
    • Chen T., Orr D.F., O'Rourke M., McLynn C., Bjourson A.J., McClean S., Hirst D., Rao P., and Shaw C. Pachymedusa dacnicolor Tryptophyllin-1: Structural Characterization, Pharmacological Activity, and Cloning of Precursor cDNA. Regul. Pept. 117 1 (2004) 25-32
    • (2004) Regul. Pept. , vol.117 , Issue.1 , pp. 25-32
    • Chen, T.1    Orr, D.F.2    O'Rourke, M.3    McLynn, C.4    Bjourson, A.J.5    McClean, S.6    Hirst, D.7    Rao, P.8    Shaw, C.9
  • 17
    • 23044466163 scopus 로고    scopus 로고
    • Bradykinin-Related Peptides and Tryptophyllins in the Skin Secretions of the Most Primitive Extant Frog, Ascaphus truei
    • Conlon J.M., Jouenne T., Cosette P., Cosquer D., Vaudry H., Taylor C.K., and Abel P.W. Bradykinin-Related Peptides and Tryptophyllins in the Skin Secretions of the Most Primitive Extant Frog, Ascaphus truei. Gen. Comp. Endocrinol. 143 2 (2005) 193-199
    • (2005) Gen. Comp. Endocrinol. , vol.143 , Issue.2 , pp. 193-199
    • Conlon, J.M.1    Jouenne, T.2    Cosette, P.3    Cosquer, D.4    Vaudry, H.5    Taylor, C.K.6    Abel, P.W.7
  • 19
    • 0036151139 scopus 로고    scopus 로고
    • Amphibian Peptides that Inhibit Neuronal Nitric Oxide Synthase. Isolation of Lesuerin from the Skin Secretion of the Australian Stony Creek Frog Litoria lesueuri
    • Doyle J., Llewellyn L.E., Brinkworth C.S., Bowie J.H., Wegener K.L., Rozek T., Wabnitz P.A., Wallace J.C., and Tyler M.J. Amphibian Peptides that Inhibit Neuronal Nitric Oxide Synthase. Isolation of Lesuerin from the Skin Secretion of the Australian Stony Creek Frog Litoria lesueuri. Eur J Biochem. 269 1 (2002) 100-109
    • (2002) Eur J Biochem. , vol.269 , Issue.1 , pp. 100-109
    • Doyle, J.1    Llewellyn, L.E.2    Brinkworth, C.S.3    Bowie, J.H.4    Wegener, K.L.5    Rozek, T.6    Wabnitz, P.A.7    Wallace, J.C.8    Tyler, M.J.9
  • 20
    • 15244355765 scopus 로고    scopus 로고
    • Antimicrobial Peptide Defenses Against Chytridiomycosis, an Emerging Infectious Disease of Amphibian Populations
    • Rollins-Smith L.A., and Conlon J.M. Antimicrobial Peptide Defenses Against Chytridiomycosis, an Emerging Infectious Disease of Amphibian Populations. Dev. Comp. Immunol. 29 7 (2005) 589-598
    • (2005) Dev. Comp. Immunol. , vol.29 , Issue.7 , pp. 589-598
    • Rollins-Smith, L.A.1    Conlon, J.M.2
  • 23
    • 33747609610 scopus 로고    scopus 로고
    • Scrambling of Sequence Information in Collision-Induced Dissociation of Peptides
    • Harrison A.G., Young A.B., Bleiholder C., Suhai S., and Paizs B. Scrambling of Sequence Information in Collision-Induced Dissociation of Peptides. J. Am. Chem. Soc. 128 32 (2006) 10364-10365
    • (2006) J. Am. Chem. Soc. , vol.128 , Issue.32 , pp. 10364-10365
    • Harrison, A.G.1    Young, A.B.2    Bleiholder, C.3    Suhai, S.4    Paizs, B.5
  • 25
    • 0028501304 scopus 로고
    • Rearrangements of Doubly Charged Acylium Ions from Lysyl and Ornithyl Peptides
    • Tang X.J., and Boyd R.K. Rearrangements of Doubly Charged Acylium Ions from Lysyl and Ornithyl Peptides. Rapid Commun. Mass Spectrom. 8 9 (1994) 678-686
    • (1994) Rapid Commun. Mass Spectrom. , vol.8 , Issue.9 , pp. 678-686
    • Tang, X.J.1    Boyd, R.K.2
  • 26
    • 0027918107 scopus 로고
    • Fragmentation Reactions of Multiply-Protonated Peptides and Implications for Sequencing by Tandem Mass Spectrometry with Low-Energy Collision-Induced Dissociation
    • Tang X.J., Thibault P., and Boyd R.K. Fragmentation Reactions of Multiply-Protonated Peptides and Implications for Sequencing by Tandem Mass Spectrometry with Low-Energy Collision-Induced Dissociation. Anal. Chem. 65 20 (1993) 2824-2834
    • (1993) Anal. Chem. , vol.65 , Issue.20 , pp. 2824-2834
    • Tang, X.J.1    Thibault, P.2    Boyd, R.K.3
  • 30
    • 34248531587 scopus 로고    scopus 로고
    • Infrared Spectroscopy and Theoretical Studies on Gas-Phase Protonated Leu-Enkephalin and Its Fragments: Direct Experimental Evidence for the Mobile Proton
    • Polfer N.C., Oomens J., Suhai S., and Paizs B. Infrared Spectroscopy and Theoretical Studies on Gas-Phase Protonated Leu-Enkephalin and Its Fragments: Direct Experimental Evidence for the Mobile Proton. J. Am. Chem. Soc. 129 18 (2007) 5887-5897
    • (2007) J. Am. Chem. Soc. , vol.129 , Issue.18 , pp. 5887-5897
    • Polfer, N.C.1    Oomens, J.2    Suhai, S.3    Paizs, B.4
  • 31
    • 41049113428 scopus 로고    scopus 로고
    • Evidence for Structural Variants of a- and b-Type Peptide Fragment Ions Using Combined Ion Mobility/Mass Spectrometry
    • Riba-Garcia I., Giles K., Bateman R.H., and Gaskell S.J. Evidence for Structural Variants of a- and b-Type Peptide Fragment Ions Using Combined Ion Mobility/Mass Spectrometry. J. Am. Soc. Mass Spectrom. 19 4 (2008) 609-613
    • (2008) J. Am. Soc. Mass Spectrom. , vol.19 , Issue.4 , pp. 609-613
    • Riba-Garcia, I.1    Giles, K.2    Bateman, R.H.3    Gaskell, S.J.4
  • 32
    • 39849088020 scopus 로고    scopus 로고
    • On the Dynamics of Fragment Isomerization in Collision-Induced Dissociation of Peptides
    • Polfer N.C., Bohrer B.C., Plasencia M.D., Paizs B., and Clemmer D.E. On the Dynamics of Fragment Isomerization in Collision-Induced Dissociation of Peptides. J. Phys. Chem. A 112 6 (2008) 1286-1293
    • (2008) J. Phys. Chem. A , vol.112 , Issue.6 , pp. 1286-1293
    • Polfer, N.C.1    Bohrer, B.C.2    Plasencia, M.D.3    Paizs, B.4    Clemmer, D.E.5
  • 33
    • 33947313512 scopus 로고    scopus 로고
    • Cyclization Reaction of Peptide Fragment Ions During Multistage Collisionally Activated Decomposition: An Inducement to Lose Internal Amino-Acid Residues
    • Jia C., Qi W., and He Z. Cyclization Reaction of Peptide Fragment Ions During Multistage Collisionally Activated Decomposition: An Inducement to Lose Internal Amino-Acid Residues. J. Am. Soc. Mass Spectrom. 18 4 (2007) 663-678
    • (2007) J. Am. Soc. Mass Spectrom. , vol.18 , Issue.4 , pp. 663-678
    • Jia, C.1    Qi, W.2    He, Z.3
  • 34
    • 0030861687 scopus 로고    scopus 로고
    • Novel Peptide Dissociation: Gas-Phase Intramolecular Rearrangement of Internal Amino Acid Residues
    • Vachet R.W., Bishop B.M., Erickson B.W., and Glish G.L. Novel Peptide Dissociation: Gas-Phase Intramolecular Rearrangement of Internal Amino Acid Residues. J. Am. Chem. Soc. 119 24 (1997) 5481-5488
    • (1997) J. Am. Chem. Soc. , vol.119 , Issue.24 , pp. 5481-5488
    • Vachet, R.W.1    Bishop, B.M.2    Erickson, B.W.3    Glish, G.L.4
  • 35
    • 0000011560 scopus 로고
    • The Effect of Collision Energy, Target Gas, and Target Gas Purity on the High Energy Collision Induced Product Ion Spectrum of Renin Substrate
    • Bordoli R.S., and Bateman R.H. The Effect of Collision Energy, Target Gas, and Target Gas Purity on the High Energy Collision Induced Product Ion Spectrum of Renin Substrate. Int. J. Mass Spectrom. Ion Processes 122 (1992) 243-254
    • (1992) Int. J. Mass Spectrom. Ion Processes , vol.122 , pp. 243-254
    • Bordoli, R.S.1    Bateman, R.H.2
  • 36
    • 0027069524 scopus 로고
    • A Novel Method for the Release and Collection of Dermal, Glandular Secretions from the Skin of Frogs
    • Tyler M.J., Stone D.J., and Bowie J.H. A Novel Method for the Release and Collection of Dermal, Glandular Secretions from the Skin of Frogs. J. Pharmacol. Toxicol. Methods 28 4 (1992) 199-200
    • (1992) J. Pharmacol. Toxicol. Methods , vol.28 , Issue.4 , pp. 199-200
    • Tyler, M.J.1    Stone, D.J.2    Bowie, J.H.3
  • 37
    • 33644841619 scopus 로고    scopus 로고
    • PhosTShunter: A Fast and Reliable Tool to Detect Phosphorylated Peptides in Liquid Chromatography Fourier Transform Tandem Mass Spectrometry Data Sets
    • Kocher T., Savitski M.M., Nielsen M.L., and Zubarev R.A. PhosTShunter: A Fast and Reliable Tool to Detect Phosphorylated Peptides in Liquid Chromatography Fourier Transform Tandem Mass Spectrometry Data Sets. J. Proteome Res. 5 3 (2006) 659-668
    • (2006) J. Proteome Res. , vol.5 , Issue.3 , pp. 659-668
    • Kocher, T.1    Savitski, M.M.2    Nielsen, M.L.3    Zubarev, R.A.4
  • 40
    • 0033594994 scopus 로고    scopus 로고
    • A Method for High-Sensitivity Peptide Sequencing Using Postsource Decay Matrix-Sssisted Laser Desorption Ionization Mass Spectrometry
    • Keough T., Youngquist R.S., and Lacey M.P. A Method for High-Sensitivity Peptide Sequencing Using Postsource Decay Matrix-Sssisted Laser Desorption Ionization Mass Spectrometry. Proc. Natl. Acad. Sci. U.S.A. 96 13 (1999) 7131-7136
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , Issue.13 , pp. 7131-7136
    • Keough, T.1    Youngquist, R.S.2    Lacey, M.P.3
  • 42
    • 0034282457 scopus 로고    scopus 로고
    • Quantitation and Facilitated de novo Sequencing of Proteins by Isotopic N-Terminal Labeling of Peptides with a Fragmentation-Directing Moiety
    • Munchbach M., Quadroni M., Miotto G., and James P. Quantitation and Facilitated de novo Sequencing of Proteins by Isotopic N-Terminal Labeling of Peptides with a Fragmentation-Directing Moiety. Anal. Chem. 72 17 (2000) 4047-4057
    • (2000) Anal. Chem. , vol.72 , Issue.17 , pp. 4047-4057
    • Munchbach, M.1    Quadroni, M.2    Miotto, G.3    James, P.4
  • 43
    • 0000789037 scopus 로고
    • Influence of Cysteine to Cysteic Acid Oxidation on the Collision-Activated Decomposition of Protonated Peptides-Evidence for Intraionic Interactions
    • Barlet O., Yang C.Y., and Gaskell S.J. Influence of Cysteine to Cysteic Acid Oxidation on the Collision-Activated Decomposition of Protonated Peptides-Evidence for Intraionic Interactions. J. Am. Soc. Mass Spectrom. 3 4 (1992) 337-344
    • (1992) J. Am. Soc. Mass Spectrom. , vol.3 , Issue.4 , pp. 337-344
    • Barlet, O.1    Yang, C.Y.2    Gaskell, S.J.3
  • 44
    • 18544362983 scopus 로고    scopus 로고
    • Identification of Degradation Products Formed During Performic Oxidation of Peptides and Proteins by High-Performance Liquid Chromatography with Matrix-Assisted Laser Desorption/Ionization and Tandem Mass Spectrometry
    • Dai J., Zhang Y., Wang J., Li X., Lu Z., Cai Y., and Qian X. Identification of Degradation Products Formed During Performic Oxidation of Peptides and Proteins by High-Performance Liquid Chromatography with Matrix-Assisted Laser Desorption/Ionization and Tandem Mass Spectrometry. Rapid Commun. Mass Spectrom. 19 9 (2005) 1130-1138
    • (2005) Rapid Commun. Mass Spectrom. , vol.19 , Issue.9 , pp. 1130-1138
    • Dai, J.1    Zhang, Y.2    Wang, J.3    Li, X.4    Lu, Z.5    Cai, Y.6    Qian, X.7
  • 45
    • 0037397184 scopus 로고    scopus 로고
    • Sulfonic Acid Derivatives for Peptide Sequencing by MALDI MS
    • Keough T., Youngquist R.S., and Lacey M.P. Sulfonic Acid Derivatives for Peptide Sequencing by MALDI MS. Anal Chem. 75 7 (2003) 156A-165A
    • (2003) Anal Chem. , vol.75 , Issue.7
    • Keough, T.1    Youngquist, R.S.2    Lacey, M.P.3
  • 46
    • 10044227382 scopus 로고    scopus 로고
    • A Case Study of de novo Sequence Analysis of N-Sulfonated Peptides by MALDI TOF/TOF Mass Spectrometry
    • Samyn B., Debyser G., Sergeant K., Devreese B., and Van Beeumen J. A Case Study of de novo Sequence Analysis of N-Sulfonated Peptides by MALDI TOF/TOF Mass Spectrometry. J. Am. Soc. Mass Spectrom. 15 12 (2004) 1838-1852
    • (2004) J. Am. Soc. Mass Spectrom. , vol.15 , Issue.12 , pp. 1838-1852
    • Samyn, B.1    Debyser, G.2    Sergeant, K.3    Devreese, B.4    Van Beeumen, J.5
  • 47
    • 33747094043 scopus 로고    scopus 로고
    • N-Terminal Amino Acid Side-Chain Cleavage of Chemically Modified Peptides in the Gas Phase: A Mass Spectrometry Technique for N-Terminus Identification
    • Chacon A., Masterson D.S., Yin H., Liebler D.C., and Porter N.A. N-Terminal Amino Acid Side-Chain Cleavage of Chemically Modified Peptides in the Gas Phase: A Mass Spectrometry Technique for N-Terminus Identification. Bioorg. Med. Chem. 14 18 (2006) 6213-6222
    • (2006) Bioorg. Med. Chem. , vol.14 , Issue.18 , pp. 6213-6222
    • Chacon, A.1    Masterson, D.S.2    Yin, H.3    Liebler, D.C.4    Porter, N.A.5


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