Axinastatin 3 as a potential anticancer agent was synthesized by chemical methods. In an electrospray ion-trap mass spectrometer, using one stage of tandem mass spectrometry (MS/MS), the linear peptide intermediate was sequenced via the complementarities of y and b ions. Then, using multistep MS/MS (to MS6), the cyclic peptide was sequenced through sequentially removing one amino acid residue in each stage of MS/MS. The difference of the fragmentation mechanisms and the sequencing approaches between them is discussed.
If the inline PDF is not rendering correctly, you can download the PDF file here.
 J.S. Davies: “The cyclization of peptides and depsipeptides”, J. Peptide Sci., Vol. 9, (2003), pp. 471–501. http://dx.doi.org/10.1002/psc.491
 G.R. Pettit, F. Gao, R.L. Cerny, D.L. Doubek, L.P. Tackett, J.M. Schmidt, and J. Chapuis: “Antineoplastic agents. 278. Isolation and structure of Axinastatins 2 and 3 from a western caroline island marine sponge”, J. Med. Chem., Vol. 37, (1994), pp. 1165–1168. http://dx.doi.org/10.1021/jm00034a014
 B.M. Souza, M.R. Marques, D.M. Tomazela, M.N. Eberlin, M.A. Mendes and M.S. Palma: “Mass spectrometric characterization of two novel inflammatory peptides from the venom of the social wasp Polybia paulista”, Rapid Commun. Mass Spectrom., Vol. 18, (2004), pp. 1095–1102. http://dx.doi.org/10.1002/rcm.1452
 W. Qi, C.X. Jia, Z.M. He and B. Qiao: “Analysis of racemization products of synthetic heptapeptide by reversed phase high performance liquid chromatography/mass spectrometry”, Chinese J. Anal. Chem., in press.
 B. Paizs and S. Suhai: “Fragmentation pathways of protonated peptides”, Mass Spec. Rev., Vol. 24, (2005), pp. 508–548. http://dx.doi.org/10.1002/mas.20024
 V.H. Wysocki, K.A. Resing, Q.F. Zhang and G.L. Cheng: “Mass spectrometry of peptides and proteins”, Methods, Vol. 35, (2005), pp. 211–222. http://dx.doi.org/10.1016/j.ymeth.2004.08.013
 L.C.M. Ngoka and M.L. Gross: “Multistep tandem mass spectrometry for sequencing cyclic peptides in an ion-trap mass spectrometer”, J. Am. Soc. Mass Spectrom., Vol. 10, (1999), pp. 732–746. http://dx.doi.org/10.1016/S1044-0305(99)00049-5
 L.C.M. Ngoka and M.L. Gross: “A nomenclature system for labeling cyclic peptides fragments”, J. Am. Soc. Mass Spectrom., Vol. 10, (1999), pp. 360–363. http://dx.doi.org/10.1016/S1044-0305(99)00006-9
 L.C.M. Ngoka, M.L. Gross and P.L. Toogood: “Sodium-directed selective cleavage of lactones: a method for structure determination of cyclodepsipeptides”, Int. J. Mass Spectrom., Vol. 182/183, (1999), pp. 289–298. http://dx.doi.org/10.1016/S1387-3806(98)14248-3
 L.C.M. Ngoka and M.L. Gross: “Multistep collisionally activated decomposition in an ion trap for the determination of the amino-acid sequence and gas-phase ion chemistry of lithium-coordinated valinomycin”, Int. J. Mass Spectrom., Vol. 194, (2000), pp. 247–259. http://dx.doi.org/10.1016/S1387-3806(99)00192-X
 L.C.M. Ngoka and M.L. Gross: “Location of alkali metal binding sites in Endothelin A selective antagonists, cylco(D-Trp-D-Asp-Pro-D-Val-Leu) and cylco(D-Trp-D-Asp-Pro-D-Ile-Leu)”, J. Mass Spectrom., Vol. 35, (2000), pp. 265–276. http://dx.doi.org/10.1002/(SICI)1096-9888(200002)35:2<265::AID-JMS946>3.0.CO;2-#
 S.M. Williams and J.S. Brodbelt: “MSn characterization of protonated cyclic peptides and metal complexes”, J. Am. Soc. Mass Spectrom., Vol. 15, (2004), pp. 1039–1054. http://dx.doi.org/10.1016/j.jasms.2004.03.015
 C.X. Jia, W. Qi, Z.M. He, H.M. Yang and B. Qiao: “Synthesis of heptapeptides and analysis of sequence by tandem ion trap mass spectrometry”, Cent. Eur. J. Chem., Vol. 4, (2006), pp. 285–298. http://dx.doi.org/10.2478/s11532-006-0004-6
 P. Roepstorff and J. Fohlmann: “Proposal for a common nomenclature for sequence ions in mass spectra of peptides”, Biomed. Mass Spectrom., Vol. 11, (1984), pp. 601–601. http://dx.doi.org/10.1002/bms.1200111109
 V.H. Wysocki, G. Tsaprailis, L.L. Smith and L.A. Breci: “Mobile and localized protons: A framework for understanding peptide dissociation”, J. Mass Spectrom., Vol. 35, (2000), pp. 1399–1406. http://dx.doi.org/10.1002/1096-9888(200012)35:12<1399::AID-JMS86>3.0.CO;2-R
 M.J. Polce, D. Ren and C. Wesdemiotis: “Dissociation of the peptide bond in protonated peptides”, J. Mass Spectrom., Vol. 35, (2000), pp. 1391–1398. http://dx.doi.org/10.1002/1096-9888(200012)35:12<1391::AID-JMS85>3.0.CO;2-1
 R.S. Johnson, S.A. Martin and K. Biemann: “Collision-induced fragmentation of (M+H)+ ions of peptides. Side chain specific sequence ions”, Int. J. Mass Spectrom. Ion Processes, Vol. 86, (1988), pp. 137–154. http://dx.doi.org/10.1016/0168-1176(88)80060-0
 M.A. Mendes, B.M. Souza, L.D. Santos and M.S. Palma: “Structural characteriztion of novel chemotactic and mastoparan peptides from the venom of the social wasp Agelaia pallipes pallipes by high-performance liquid chromatography/electrospray ionization tandem mass spectrometry”, Rapid Commun. Mass Specrom., Vol. 18, (2004), pp. 636–642. http://dx.doi.org/10.1002/rcm.1382
 R.W. Vachet, B.M. Bishop, B.W. Erickson and G.L. Glish: “Novel peptide dissociation: Gas-phase intramolecular rearrangement of internal amino acid residues”, J. Am. Chem. Soc., Vol. 119, (1997), pp. 5481–5488. http://dx.doi.org/10.1021/ja9640758
 P. Stefanowicz: “Electrospray mass spectrometry and tandem mass spectrometry of the matural mixture of cyclic peptides from linseed”, Eur. J. Mass Spectrom., Vol. 10, (2004), pp. 665–671. http://dx.doi.org/10.1255/ejms.657
 B. Paizs, M. Schnolzer, U. Warnken and S. Suhai: “Cleavage of the amide bond of protonated dipeptides”, Phys. Chem. Chem. Phys., Vol. 6, (2004), pp. 2691–2699. http://dx.doi.org/10.1039/b315597h
Open Chemistry is a peer-reviewed, open access journal that publishes original research, reviews and short communications in the fields of chemistry in an ongoing way. Our central goal is to provide a hub for researchers working across all subjects to present their discoveries, and to be a forum for the discussion of the important issues in the field.