Sequencing of T-Superfamily Conotoxins from Conus virgo: Pyroglutamic Acid Identification and Disulfide Arrangement by MALDI Mass Spectrometry

Journal of the American Society for Mass Spectrometry

Volumn 18, Issue 8, 2007, Pages 1396-1404

  Mandal, Amit Kumar ^a   Ramasamy, Mani Ramakrishnan Santhana ^b   Sabareesh, Varatharajan ^a   Openshaw, Matthew E ^c   Krishnan, Kozhalmannom S ^b,d   Balaram, Padmanabhan ^a  

^a INDIAN INSTITUTE OF SCIENCE   (India)

^b TATA INSTITUTE OF FUNDAMENTAL RESEARCH   (India)

^c Shimadzu Biotech   (United Kingdom)

^d TATA INSTITUTE OF FUNDAMENTAL RESEARCH   (India)

Author keywords

[No Author keywords available]

Indexed keywords

CONUS PEPTIDES; DISULFIDE ARRANGEMENT; DISULFIDE BONDS; ENZYMATIC CLEAVAGE; MATRIX ASSISTED LASER DESORPTION IONIZATION; PYROGLUTAMIC ACID; PYROGLUTAMYL RESIDUE; SEQUENCING; T-SUPERFAMILY CONOTOXINS; VERMIVOROUS CONE SNAIL;

AROMATIC HYDROCARBONS; CHEMICAL BONDS; CHEMICAL MODIFICATION; DISSOCIATION; ESTERIFICATION; HYDROLYSIS; MASS SPECTROMETRY;

PEPTIDES;

CONOTOXIN; CYSTEINE; PYROGLUTAMIC ACID;

ACETYLATION; ALKYLATION; ARTICLE; CHEMICAL MODIFICATION; COLLISIONALLY ACTIVATED DISSOCIATION; DISULFIDE BOND; ESTERIFICATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HYDROLYSIS; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; PROTEIN DEGRADATION; PROTEIN PURIFICATION; REDUCTION; SEQUENCE ANALYSIS; SNAIL;

AMINO ACID SEQUENCE; ANIMALS; CONOTOXINS; CONUS SNAIL; PYRROLIDONECARBOXYLIC ACID; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

CONUS VIRGO; GASTROPODA;

EID: 34447639984     PISSN: 10440305     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jasms.2007.04.009     Document Type: Article

References (31)

1. Sabareesh V., Hanumae-Gowd K., Ramasamy P., Sudarslal S., Krishnan K.S., Sikdar S.K., and Balaram P. Characterization of Contryphans from Conus loroisi and Conus amadis that Target Calcium Channels. Peptides 27 (2006) 2647-2654
2. Quinton L., Le Caer J.-P., Vinh J., Gilles N., and Chamot-Rooke J. Fourier Transform Mass Spectrometry: A Powerful Tool for Toxin Analysis. Toxicon 47 (2006) 715-726
3. Gowd K.H., Sabareesh V., Sudarslal S., Iengar P., Franklin B., Fernando A., Dewan K., Ramaswami M., Sarma S.P., Sikdar S., Balaram P., and Krishnan K.S. Novel Peptides of Therapeutic Promise from Indian Conidae. Ann. N.Y. Acad. Sci 1056 (2005) 462-473
4. Sudarslal S., Singaravadivelan G., Ramasamy P., Ananda K., Sarma S.P., Sikdar S.K., Krishnan K.S., and Balaram P. A Novel 13 Residue Acyclic Peptide from the Marine Snail, Conus monile, Targets Potassium Channels. Biochem. Biophys. Res. Commun 317 (2004) 682-688
5. Jakubowski J.A., and Sweedler J.V. Sequencing and Mass Profiling Highly Modified Conotoxins Using Global Reduction/Alkylation Followed by Mass Spectrometry. Anal. Chem 76 (2004) 6541-6547
6. Peng J., and Gygi S.P. Proteomics: The Move to Mixtures. J. Mass Spectrom 36 (2001) 1083-1091
7. Aebersold R., and Mann M. Mass Spectrometry-Based Proteomics. Nature 422 (2003) 198-207
8. Sarma S.P., Senthil Kumar G., Sudarslal S., Iengar P., Ramasamy P., Sikdar S.K., Krishnan K.S., and Balaram P. Solution Structure of δ-Am2766: A Highly Hydrophobic δ-Conotoxin from Conus amadis that Inhibits Inactivation of Neuronal Voltage Gated Sodium Channels. Chem. Biodiv 2 (2005) 535-556
9. Sudarslal S., Majumdar S., Ramasamy P., Dhawan R., Pal P.P., Ramaswami M., Lala A.K., Sikdar S.K., Sarma S.P., Krishnan K.S., and Balaram P. Sodium Channel Modulating Activity in a δ-Conotoxin from an Indian marine snail. FEBS Lett 553 (2003) 209-212
10. Kim T.Y., Brun Y.V., and Reilly J.P. Effects of Tryptic Peptide Esterification in MALDI Mass Spectrometry. Anal. Chem 77 (2005) 4185-4193
11. Kinter M., and Sherman N.E. Post-Translationally Modified Neuropeptides from Conus venoms. Eur. J. Biochem. 264 (1999) 271-275
12. Kinter M., and Sherman N.E. Protein Sequencing and Identification Using Tandem Mass Spectrometry (2000), Wiley-Interscience on Mass Spectrometry, New York 149
13. Johnson R.S., Martin S.A., Biemann K., Stults J.T., and Watson J.T. Novel Fragmentation Process of Peptides by Collision-Induced Decomposition in a Tandem Mass Spectrometer: Differentiation of Leucine and Isoleucine. Anal. Chem 59 (1987) 2621-2625
14. Aguilar M.B., Lezama-Monfil L., Maillo M., Pedraza-Lara H., Lopez-Vera E., and Heimer-de la Cotera E.P. A Biologically Active Hydrophobic T-1-Conotoxin from the Venom Conus spurious. Peptides 27 (2006) 500-505
15. Jakubowski J.A., Kelly W.P., and Sweedler J.V. Screening for Post-Translational Modifications in Conotoxins Using Liquid Chromatography/Mass Spectrometry: An important component of conotoxin discovery. Toxicon 47 (2006) 688-699
16. Nair S.S., Nilsson C.L., Emmett M.R., Schaub T.M., Gowd K.H., Thakur S.S., Krishnan K.S., Balaram P., and Marshall A.G. De Novo Sequencing and Disulfide Mapping of a Bromotryptophan-Containing Conotoxins by Fourier Transform Ion Cyclotron Resonance Mass Spectrometry. Anal. Chem 78 (2006) 8082-8088
17. Luo S., Zhangsun D., Zhang B., Chen X., and Feng J. Direct cDNA Cloning of Novel Conotoxins of the T-Superfamily from Conus textile. Peptides 27 (2006) 2640-2646
18. Chen W.-H., Han Y.-H., Wang Q., Miao X.-W., Ou L., and Shao X.-X. cDNA Cloning of Two Novel T-Superfamily Conotoxins from Conus leopardus. Acta Biochim. Biophys. Sin 38 (2006) 287-291
19. Han Y.H., Wang Q., Jiang H., Miao X.W., Chen J.S., and Chi C.W. Sequence Diversity of T-Superfamily Conotoxins from Conus marmoreus. Toxicon 45 (2005) 481-487
20. Jakubowski J.A., Keays D.A., Kelly W.P., Sandall D.W., Bingam J.-P., Livett B.G., Gayler K.R., and Sweedler J.V. Determining Sequences and Post-Translational Modifications of Novel Conotoxins in Conus victoriae Using cDNA Sequencing and Mass Spectrometry. J. Mass Spectrom 39 (2004) 548-557
21. Hansson K., Furie B., Furie B.C., and Stenflo J. Isolation and Characterization of Three Novel Gla-Containing Conus marmoreous Venom Peptides, One with a Novel Cysteine Pattern. Biochem. Biophys. Res. Commun 319 (2004) 1081-1087
22. Kalume D.E., Stenflo J., Czerwiec E., Hambe B., Furie B.C., Furie B., and Roepstorff P. Structure Determination of Two Conotoxins from Conus Textile by a Combination of Matrix Assisted Laser Desorption/Ionization Time of Flight and Electrospray Ionization Mass Spectrometry and Biochemical Methods. J. Mass Spectrom 35 (2000) 145-156
23. 2+ Influx. Proc. Natl. Acad. Sci. U.S.A. 96 (1999) 5758-5763
24. Walker C.S., Steel D., Jacobsen R.D., Lirazan M.B., Cruz L.J., Hooper D., Shetty R., DelaCruz R.C., Nielsen J.S., Zhou L.M., Bandopadhayay P., Craig A.G., and Olivera B.M. The T-Super Family of Conotoxins. J Biol. Chem 274 (1999) 30664-30671
25. McIntosh J.M., Corpuz G.O., Layer R.T., Garrett J.E., Wagstaff J.D., Bulaj G., Vyzovkina, Yoshikami D., Cruz L.J., and Olivera B.M. Isolation and Characterization of a novel Conus Peptide with Apparent Antinociceptive activity. J. Biol. Chem 275 (2000) 32391-32397
26. Balaji R.A., Ohtake A., Sato K., Gopalakrishnakone P., Kini R.M., Seow K.T., and Bay B.H. λ-Conotoxins, a New Family with Unique Disulphide Pattern and Protein Folding: Isolation and Characterization from the Venom of Conus marmoreus. J. Biol. Chem 275 (2000) 39516-39522
27. Sharpe I.A., Gehrmann J., Loughnan M.L., Thomas L., Adams D.A., Atkins A., Palant E., Craik D.J., Alewood P.F., and Lewis R.J. Two New Classes of Conopeptides Inhibit the α-1 Adrenoceptor and Noradrenaline Transporter. Nat. Neurosci 4 (2001) 902-907
28. Craig A.G., Jimenez E.C., Dykert J., Nielsen D.B., Gulyas J., Abogadie F.C., Porter J., Rivier J.E., Cruz L.J., Olivera B.M., and McIntosh J.M. A Novel Post-Translational Modification Involving Bromination of Tryptophan. Identification of the Residue, L-6-Bromotryptophan, in Peptides from Conus imperialis and Conus radiatus venom. J. Biol. Chem 272 (1997) 4689-4698
29. Kjeldsen F., Haselmann K.F., Budnik B.A., Jensen F., and Zubarev R.A. Dissociative Capture of Hot (3-13 eV) Electrons by Polypeptide Polycations: An Efficient Process Accompanied by Secondary Fragmentation. Chem. Phys. Lett 356 (2002) 201-206
30. Kjeldsen F., Haselmann K.F., Sorensen E.S., and Zubarev R.A. Distinguishing of Ile/Leu Amino Acid Residues in the PP3 Protein by (Hot) Electron Capture Dissociation in Fourier Transform Ion Cyclotron Resonance Mass Spectrometry. Anal. Chem 75 (2003) 1267-1274
31. Medzihradszky K.F. Peptide Sequence Analysis. Methods Enzymol 402 (2005) 209-244