Characterization of Alkali Induced Formation of Lanthionine, Trisulfides, and Tetrasulfides from Peptide Disulfides using Negative Ion Mass Spectrometry

Journal of the American Society for Mass Spectrometry

Volumn 20, Issue 5, 2009, Pages 783-791

  Thakur, Suman S ^a   Balaram, Padmanabhan ^a  

^a INDIAN INSTITUTE OF SCIENCE   (India)

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE CONDITIONS; ALKALINE MEDIAS; CLEAVAGE REACTIONS; CYCLIC PEPTIDES; CYCLIC PRODUCTS; CYS RESIDUES; ELECTROSPRAY IONIZATION MASS SPECTROMETRIES; GLUTATHIONE; INTERMEDIATE SPECIES; LANTHIONINE; MASS SPECTRAL EVIDENCES; MASS SPECTRAL FRAGMENTATIONS; MICHAEL ADDITION REACTIONS; NEGATIVE ION; THIOL GROUPS; THIOL SPECIES; TRAPPING METHODS;

ADDITION REACTIONS; ELECTROSPRAY IONIZATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HYDROCARBONS; MASS SPECTROMETERS; MASS SPECTROMETRY; NEGATIVE IONS; PEPTIDES; POLYSULFIDES; SPECTRUM ANALYSIS;

AMINES;

ALKALI; CYSTEINE; DEHYDROALANINE; GLUTATHIONE; LANTHIONINE; PEPTIDE DISULFIDE DERIVATIVE; PROTON; SULFIDE; TETRASULFIDE DERIVATIVE; THIOL; TRISULFIDE DERIVATIVE; UNCLASSIFIED DRUG;

ALKYLATION; ARTICLE; CHEMICAL STRUCTURE; ELECTROSPRAY MASS SPECTROMETRY; ELIMINATION REACTION; MASS SPECTROMETRY; MICHAEL ADDITION; OXIDATION;

ALANINE; GLUTATHIONE DISULFIDE; PEPTIDES, CYCLIC; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; SULFHYDRYL COMPOUNDS; SULFIDES;

EID: 64049088076     PISSN: 10440305     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jasms.2008.12.019     Document Type: Article

References (59)

1. Brown J.R., and Hartley B.S. Location of Disulphide Bridges by Diagonal Paper Electrophoresis. The Disulphide Bridges of Bovine Chymotrypsinogen A. Biochem. J. 101 (1966) 214-228
2. Pinck J.R., and Milstein C. Disulphide Bridges of a Human Immunoglobulin G Protein. Nature 216 (1967) 941-942
3. Gray W.R. Disulfide Structures of Highly Bridged Peptides: A New Strategy for Analysis. Protein Sci. 10 (1993) 1732-1748
4. Gorman J.J., Wallis T.P., and Pitt J.J. Protein Disulfide Bond Determination by Mass Spectrometry. Mass Spectrom. Rev. 21 (2002) 183-216
5. Yen T.Y., Yan H., and Macher B.A. Characterizing Closely Spaced, Complex Disulfide Bond Patterns in Peptides and Proteins by Liquid Chromatography/Electrospray Ionization Tandem Mass Spectrometry. J. Mass Spectrom. 37 (2002) 15-30
6. Gunawardena H.P., O'Hair R.A., and McLuckey S.A. Selective Disulfide Bond Cleavage in Gold (I) Cationized Polypeptide Ions Formed Via Gas-Phase Ion/Ion Cation Switching. J. Proteome Res. 5 (2006) 2087-2092
7. Lioe H., and O'Hair R.A. A Novel Salt Bridge Mechanism Highlights the Need for Nonmobile Proton Conditions to Promote Disulfide Bond Cleavage in Protonated Peptides under Low-Energy Collisional Activation. J. Am. Soc. Mass Spectrom. 18 (2007) 1109-1123
8. Lioe H., Duan M., and O'Hair R.A. Can Metal Ions be Used as Gas-Phase Disulfide Bond Cleavage Reagents?. A Survey of Coinage Metal Complexes of Model Peptides Containing an Intermolecular Disulfide Bond. Rapid Commun. Mass Spectrom. 21 (2007) 2727-2733
9. Thakur S., and Balaram P. Rapid Mass Spectral Identification of Contryphans. Detection of Characteristic Peptide Ions by Fragmentation of Intact Disulfide Bonded Peptides in Crude Venom. S.;. Rapid Commun. Mass Spectrom. 21 (2007) 3420-3426
10. Kim H.I., and Beauchamp J.L. Identifying the Presence of a Disulfide Linkage in Peptides by the Selective Elimination of Hydrogen Disulfide from Collisionally Activated Alkali and Alkaline Earth Metal Complexes. J. Am. Chem. Soc. 130 (2008) 1245-1257
11. Kim H.I., and Beauchamp J.L. Mapping Disulfide Bonds in Insulin with the Route 66 Method: Selective Cleavage of S-C Bonds Using Alkali and Alkaline Earth Metal Enolate Complexes. J. Am. Soc. Mass Spectrom. (2008), online in press, doi:10.1016/j.jasms. 2008.10.003.
12. Martinez T., Guo A., Allen M.J., Han M., Pace D., Jones J., Gillespie R., Ketchem R.R., Zhang Y., and Balland A. Disulfide Connectivity of Human Immunoglobulin G2 Structural Isoforms. Biochemistry 47 (2008) 7496-7508
13. Jai-nhuknan J., and Cassady C.J. Negative Ion Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Post-Source Decay Calibration by Using Fibrinopeptide B. J. Am. Soc. Mass Spectrom. 9 (1998) 540-544
14. Jai-nhuknan J., and Cassady C.J. Negative Ion Postsource Decay Time-of-Flight Mass Spectrometry of Peptides Containing Acidic Amino Acid Residues. Anal. Chem. 70 (1998) 5122-5128
15. Ewing N.P., and Cassady C.J. Dissociation of Multiply Charged Negative Ions for Hirudin (54-65), Fibrinopeptide B, and Insulin A (Oxidized). J. Am. Soc. Mass Spectrom. 12 (2001) 105-116
16. Bowie J.H. Recent Advances in Negative Ion Mass Spectrometry. Environ. Health Perspect. 36 (1980) 89-95
17. Bradford A.M., Waugh R.J., and Bowie J.H. Characterization of Underivatized Tetrapeptides by Negative-Ion Fast-Atom Bombardment Mass Spectrometry. Rapid Commun. Mass Spectrom. 9 (1995) 677-685
18. - Ions of Phenylthiohydantoin Leu and Ile. Rapid Commun. Mass Spectrom. 9 (1995) 1241-1243
19. Steinborner S.T., and Bowie J.H. A Comparison of the Positive- and Negative-ion Mass Spectra of Bioactive Peptides from the Dorsal Secretion of the Australian Red Tree Frog. Litoria rubella. Rapid Commun. Mass Spectrom. 10 (1996) 1243-1247
20. Brinkworth C.S., Dua S., McAnoy A.M., and Bowie J.H. Negative Ion Fragmentations of Deprotonated Peptides: Backbone Cleavages Directed Through Both Asp and Glu. Rapid Commun. Mass Spectrom. 15 (2001) 1965-1973
21. Boontheung P., Alewood P.F., Brinkworth C.S., Bowie J.H., Wabnitz P.A., and Tyler M.J. Negative Ion Electrospray Mass Spectra of Caerulein Peptides: An Aid to Structural Determination. Rapid Commun. Mass Spectrom. 16 (2002) 281-286
22. Brinkworth C.S., Dua S., and Bowie J.H. Backbone cleavages of [M - H](-) anions of peptides. Cyclization of Citropin 1 Peptides Involving Reactions Between the C-Terminal [CONH](-) Residue and Backbone Amide Carbonyl Groups. A New Type of β Cleavage: A Joint Experimental and Theoretical Study. Rapid Commun. Mass Spectrom. 16 (2002) 713-721
23. Brinkworth C.S., and Bowie J.H. Backbone Cleavages of [M - H](-) Anions Derived from Caerin 1 Peptides and Some Synthetic Modifications. Molecular Recognition Initiating Internal Cyclization of Glu23. Rapid Commun. Mass Spectrom. 16 (2002) 1339-1351
24. - Parent Anions of Underivatized Peptides: An Aid to Structure Determination and Some Unusual Negative Ion Cleavages. Mass Spectrom. Rev. 21 (2002) 87-107 Review.
25. Bowie J.H., Peppe S., Dua S., and Blanksby S.J. Formation of Neutral Molecules of Potential Stellar Interest by Neutralization of Negative Ions in a Mass Spectrometer. The Application of Experiment and Molecular Modeling in Concert. J. Mol. Graph. Model. 21 (2003) 357-364
26. Brinkworth C.S., and Bowie J.H. Negative Ion Electrospray Mass Spectra of the Maculatin Peptides from the Tree Frogs Litoria genimaculata and Litoria eucnemis. Rapid Commun. Mass Spectrom. 17 (2003) 2215-2225
27. Brinkworth C.S., Bowie J.H., Bilusich D., and Tyler M.J. The Rothein Peptides from the Skin Secretion of Roth's Tree Frog Litoria Rothii. Sequence Determination Using Positive and Negative Ion Electrospray Mass Spectrometry. Rapid Commun. Mass Spectrom. 19 (2005) 2716-2724
28. Maclean M.J., Brinkworth C.S., Bilusich D., Bowie J.H., Doyle J.R., Llewellyn L.E., and Tyler M.J. New Caerin Antibiotic Peptides from the Skin Secretion of the Dainty Green Tree Frog Litoria gracilenta. Identification Using Positive and Negative Ion Electrospray Mass Spectrometry. Toxicon. 47 (2006) 664-675
29. Jackway R.J., Bowie J.H., Bilusich D., Musgrave I.F., Surinya-Johnson K.H., Tyler M.J., and Eichinger P.C. The Fallaxidin Peptides from the Skin Secretion of the Eastern Dwarf Tree Frog Litoria fallax. Sequence Determination by Positive and Negative Ion Electrospray Mass Spectrometry: Antimicrobial Activity and cDNA Cloning of the Fallaxidins. Rapid Commun. Mass Spectrom. 22 (2008) 3207-3216
30. 2S from Cys. A Joint Experimental and Theoretical Study. Rapid Commun. Mass Spectrom. 17 (2003) 2488-2494
31. Bilusich D., Brinkworth C.S., and Bowie J.H. Negative Ion Mass Spectra of Cys-Containing Peptides. The Characteristic Cys γ Backbone Cleavage: A Joint Experimental and Theoretical Study. Rapid Commun. Mass Spectrom. 18 (2004) 544-552
32. Maselli V.M., Brinkworth C.S., Bowie J.H., and Tyler M.J. Host-Defense Skin Peptides of the Australian Common Froglet Crinia signifera: Sequence Determination Using Positive and Negative Ion Electrospray Mass Spectra. Rapid Commun. Mass Spectrom. 18 (2004) 2155-2161
33. Bilusich D., Maselli V.M., Brinkworth C.S., Samguina T., Lebedev A.T., and Bowie J.H. Direct Identification of Intramolecular Disulfide Links in Peptides Using Negative Ion Electrospray Mass Spectra of Underivatized Peptides. A Joint Experimental and Theoretical Study. Rapid Commun. Mass Spectrom. 19 (2005) 3063-3074
34. Maselli V.M., Bilusich D., Bowie J.H., and Tyler M.J. Host-Defense Skin Peptides of the Australian Streambank Froglet Crinia riparia: Isolation and sequence determination by positive and negative ion electrospray mass spectrometry. Rapid Commun. Mass Spectrom. 20 (2006) 797-803
35. Biluisch D., and Bowie J.H. Identification of Intermolecular Disulfide Linkages in Underivatized Peptides Using Negative Ion Electrospray Mass Spectrometry. A Joint Experimental and Theoretical Study. Rapid Commun. Mass Spectrom. 21 (2007) 619-628
36. Zhang M., and Kaltashov I.A. Mapping of Protein Disulfide Bonds Using Negative Ion Fragmentation with a Broadband Precursor Selection. Anal. Chem. 78 (2006) 4820-4829
37. Chelius D., Wimer M.E.H., and Bondarenko P.V. Reversed-Phase Liquid Chromatography In-Line with Negative Ionization Electrospray Mass Spectrometry for the Characterization of the Disulfide-Linkages of an Immunoglobulin γ Antibody. J. Am. Soc. Mass Spectrom. 11 (2006) 1590-1598
38. Thakur S.S., and Balaram P. Fragmentation of Peptide Disulfides under Conditions of Negative Ion Mass Spectrometry: Studies of Oxidized Glutathione and Contryphan. J. Am. Soc. Mass Spectrom. 19 (2008) 358-366
39. Galande A.K., and Spatola A.F. A Facile Method for the Direct Synthesis of Lanthionine Containing Cyclic Peptides. Lett. Peptide Sci. 8 (2002) 247-251
40. Galande A.K., Trent J.O., and Spatola A.F. Understanding Base-Assisted Desulfurization Using a Variety of Disulfide-Bridged Peptides. Biopolymers 71 (2003) 534-551
41. Parker A.J., and Kharasch N. The Science of the Sulfur-Sulfur bond. Chem. Rev. 59 (1959) 583-628
42. Horn M.J., Jones D.B., and Ringel S.J. Isolation of a New Sulfur-Containing Amino Acid (lanthionine) from Sodium Carbonate-Treated Wool. J. Biol. Chem. 138 (1941) 141-149
43. Horn M.J., Jones D.B., and Ringel S.J. Isolation of Mesolanthionine from Various Alkali-Treated Proteins. J. Biol. Chem. 144 (1942) 87-91
44. Speakman J.B. Reactivity of the Sulphur Linkage in Wool. Nature (1933) 132, 930.
45. Hylin J.W., and Wood J.L. Enzymatic Formation of Polysulfides from Mercaptopyruvate. J. Biol. Chem. 234 (1959) 2141-2144
46. Fletcher J.C., and Robson A. The Occurrence of Bis-(2-Amino-2-Carboxyethyl) Trisulphide in Hydrolysates of Wool and Other Proteins. Biochem. J. 87 (1963) 553-559
47. Wood J.L., and Catsimpoolas N. Cleavage of the Peptide Bond at the Cystine Amino Group by the Action of Cyanide. J. Biol. Chem. 238 (1963) 2887-2888
48. Donovan J.W. Spectrophotometric Observation of the Alkaline Hydrolysis of Protein Disulfide Bonds. Biochem. Biophys. Res. Commun. (1967) 734-740 29, 5.
49. Schneider J.F., and Westley J. Metabolic Interrelations of Sulfur in Proteins, Thiosulfate, and Cystine. J. Biol. Chem. 244 (1969) 5735-5744
50. Nashef A.S., Osuga D.T., Lee H.S., Ahmed A.I., Whitaker J.R., and Feeney R.E. Effects of Alkali on Proteins. Disulfides and Their Products. J. Agric. Food. Chem. 25 (1977) 245-251
51. Florence T.M. Degradation of Protein Disulphide Bonds in Dilute Alkali. Biochem. J. 189 (1980) 507-520
52. Jones A.J., Helmerhorst E., and Stokes G.B. The Formation of Dehydroalanine Residues in Alkali-Treated Insulin and Oxidized Glutathione. A Nuclear-Magnetic-Resonance Study. Biochem. J. 211 (1983) 499-502
53. Zviak C. The Science of Hair Care (1986), Informa Health Care, London, UK 185-186
54. Catsimpoolas N., and Wood J.L. The Reaction of Cyanide with Bovine Serum Albumin. J. Biol. Chem. 239 (1964) 4132-4137
55. Canova-Davis E., Baldonado I.P., Chloupek R.C., Ling V.T., Gehant R., Olson K., and Gillece-Castro B.L. Confirmation by Mass Spectrometry of a Trisulfide Variant in Methionyl Human Growth Hormone Biosynthesized in Escherichia coli. Anal. Chem. 68 (1996) 4044-4051
56. Jespersen A.M., Christensen T., Klausen N.K., Nielsen F., and Sørensen H.H. Characterization of a Trisulphide Derivative of Biosynthetic Human Growth Hormone Produced in Escherichia coli. Eur. J. Biochem. 219 (1994) 365-373
57. Ravi A., and Balaram P. Stabilization of β-Turn Conformations in Pro-X Sequences by Disulfide Bridging. Synthesis and Solution Conformations of Five Cyclic Cystine Peptides. Tetrahedron 40 (1984) 2577-2583
58. Tardif S.L., Rys A.Z., Abrams C.B., Abu-Yousef I.A., Lesté-Lasserre P.B.F., Schultz E.K.V., and Harpp D.N. Recent Chemistry of the Chalcogen Diatomics. Tetrahedron 53 (1997) 12225-12236
59. Zysman-Colman E., and Harpp D.N. Fascinating organo Sulfur Functionalities: Polychalcogens as Diatomic Sulfur Sources. Heteroatom Chem. 18 (2007) 449-459