A New Method for Analysis of Disulfide-Containing Proteins by Matrix-Assisted Laser Desorption Ionization (MALDI) Mass Spectrometry

Journal of the American Society for Mass Spectrometry

Volumn 20, Issue 12, 2009, Pages 2284-2293

  Yang, Hongmei ^a,b   Liu, Ning ^a,c   Qiu, Xiaoyan ^a   Liu, Shuying ^a,d  

^a CHANGCHUN INSTITUTE OF APPLIED CHEMISTRY   (China)

^b UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

^c JILIN UNIVERSITY   (China)

^d CHANGCHUN UNIVERSITY OF CHINESE MEDICINE   (China)

Author keywords

[No Author keywords available]

Indexed keywords

ADDUCT ION; ALKALINE CONDITIONS; CAFFEIC ACIDS; CHEMICAL REDUCTION; CYANO-4-HYDROXYCINNAMIC ACIDS; CYSTEINE RESIDUES; DISULFIDE BONDS; DISULFIDE BRIDGE; FERULIC ACIDS; HIGH-THROUGHPUT METHOD; MALDI-MASS SPECTROMETRY; MASS SHIFT; MASS SPECTRA; MATRIX; MATRIX-ASSISTED LASER DESORPTION IONIZATION; PROTEINS/PEPTIDES; SINAPINIC ACID; SULFHYDRYL GROUPS; UNDERLYING MECHANISM;

ACIDS; ADDITION REACTIONS; AMINES; DESORPTION; MASS SPECTROMETERS; MASS SPECTROMETRY; PEPTIDES;

MATRIX ALGEBRA;

2 (4 HYDROXYPHENYLAZO)BENZOIC ACID; ALPHA CYANO 4 HYDROXYCINNAMIC ACID; CAFFEIC ACID; CYSTEINE; DISULFIDE; DITHRANOL; FERULIC ACID; PICOLINIC ACID DERIVATIVE; PROTEIN; SINAPIC ACID; SODIUM ION; THIOL GROUP;

ALKALINITY; AMINO ACID COMPOSITION; ARTICLE; CHEMICAL STRUCTURE; CONTROLLED STUDY; DISULFIDE BOND; ELECTROSPRAY MASS SPECTROMETRY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; MOLECULAR WEIGHT; PROTEIN ANALYSIS; PROTEIN DEGRADATION;

ALGORITHMS; DISULFIDES; PROTEINS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

EID: 70449502844     PISSN: 10440305     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jasms.2009.08.020     Document Type: Article

References (38)

1. Lehle K., Kohnert U., Stern A., Popp F., and Jaenicke R. Effect of Disulfide Bonds on the Structure, Function, and Stability of the Trypsin/tPA Inhibitor from Erythrina caffra: Site-Directed Mutagenesis, Expression, and Physiochemical Characterization. Nat. Biotechol. 14 (1996) 476-480
2. Wedemeyer W.J., Welker E., Narayan M., and Scheraga H.A. Disulfide Bonds and Protein Folding. Biochemistry 39 (2000) 4207-4216
3. Reinders J., and Sickmann A. Modificomics: Post-translational Modifications Beyond Protein Phosphorylation and Glycosylation. Biomol. Eng. 24 (2007) 169-177
4. Walewska A., Skalicky J.J., Davis D.R., Zhang M.M., Lopez-Vera E., Watkins M., Han T.S., Yoshikami D., Olivera B.M., and Bulaj G. NMR-Based Mapping of Disulfide Bridges in Cysteine-Rich Peptides: Application to the μ-Conotoxin SxIIIA. J. Am. Chem. Soc. 130 (2008) 14280-14286
5. von Ossowski L., Tossavainen H., von Ossowski I., Cai C., Aitio O., Fredriksson K., Permi P., Annila A., and Keinänen K. Peptide Binding and NMR Analysis of the Interaction between SAP97 PDZ2 and GluR-A: Potential Involvement of a Disulfide Bond. Biochemistry 45 (2006) 5567-5575
6. Collins E.S., Wirmer J., Hirai K., Tachibana H., Segawa S., Dobson C.M., and Schwalbe H. Characterization of Disulfide-Bond Dynamics in Non-Native States of Lysozyme and Its Disulfide Deletion Mutants by NMR. Chem biochem. 6 (2005) 1619-1627
7. Chait B.T., and Field F.H. A Rapid, Sensitive Mass Spectrometric Method for Investigating Microscale Chemical Reactions of Surface Adsorbed Peptides and Proteins. Biochem. Biophys. Res. Commun. 134 (1986) 420-426
8. Patterson S.D., and Katta V. Prompt Fragmentation of Disulfide-Linked Peptides during Matrix-Assisted Laser Desorption Ionization Mass Spectrometry. Anal. Chem. 66 (1994) 3727-3732
9. Huwiler K.G., Mosher D.F., and Vestling M.M. Optimizing the MALDI-TOF-MS Observation of Peptides Containing Disulfide Bonds. J. Biomol. Tech. 14 (2003) 289-297
10. Foley S.F., Sun Y., Zheng T.S., and Wen D. Picomole-Level Mapping of Protein Disulfides by Mass Spectrometry Following Partial Reduction and Alkylation. Anal. Biochem. 377 (2008) 95-104
11. Schnaible V., Wefing S., Bücker A., Wolf-Kümmeth S., and Hoffmann D. Partial Reduction and Two-Step Modification of Proteins for Identification of Disulfide Bonds. Anal. Chem. 74 (2002) 2386-2393
12. Wu W., Huang W., Qi J., Chou Y.T., Torng E., and Watson J.T. 'Signature Sets', Minimal Fragment Sets for Identifying Protein Disulfide Structures with Cyanylation-Based Mass Mapping Methodology. J. Proteome Res. 3 (2004) 770-777
13. Qi J., Wu W., Borges C.R., Hang D., Rupp M., Torng E., and Watson J.T. Automated Data Interpretation Based on the Concept of "Negative Signature Mass" for Mass-Mapping Disulfide Structures of Cystinyl Proteins. J. Am. Soc. Mass Spectrom. 14 (2003) 1032-1038
14. Fukuyama Y., Iwamoto S., and Tanaka K. Rapid Sequencing and Disulfide Mapping of Peptides Containing Disulfide Bonds by Using 1,5-Diaminonaphthalene as a Reductive Matrix. J. Mass Spectrom. 41 (2006) 191-201
15. Quinton L., Demeure K., Dobson R., Gilles N., Gabelica V., and De Pauw E. New Method for Characterizing Highly Disulfide-Bridged Peptides in Complex Mixtures: Application to Toxin Identification from Crude Venoms. J. Proteome Res. 6 (2007) 3216-3223
16. Demeure K., Quinton L., Gabelica V., and De Pauw E. Rational Selection of the Optimum MALDI Matrix for Top-Down Proteomics by In-Source Decay. Anal. Chem. 79 (2007) 8678-8685
17. 1 Ion Recognition. Anal. Chem. 80 (2008) 9135-9140
18. Schnaible V., Wefing S., Resemann A., Suckau D., Bücker A., Wolf-Kümmeth S., and Hoffmann D. Screening for Disulfide Bonds in Proteins by MALDI In-Source Decay and LIFT-TOF/TOF-MS. Anal. Chem. 74 (2002) 4980-4988
19. 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
20. 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
21. 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
22. Mihalca R., van der Burgt Y.E., Heck A.J., and Heeren R.M. Disulfide Bond Cleavages Observed in SORI-CID of Three Nonapeptides Complexed with Divalent Transition-Metal Cations. J. Mass Spectrom. 42 (2007) 450-458
23. Kim H.I., and Beauchamp J.L. Mapping Disulfide Bonds in Insulin with the Route 66 Method: Selective Cleavage of SOC Bonds Using Alkali and Alkaline Earth Metal Enolate Complexes. J. Am. Soc. Mass Spectrom. 20 (2009) 157-166
24. 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
25. King G.J., Jones A., Kobe B., Huber T., Mouradov D., Hume D.A., and Ross I.L. Identification of Disulfide-Containing Chemical Cross-Links in Proteins Using MALDI-TOF/TOF-Mass Spectrometry. Anal. Chem. 80 (2008) 5036-5043
26. 1 Chain N-terminal Domains by Nano-High-Performance Liquid Chromatography/Matrix-Assisted Laser Desorption/Ionization Time-of-Flight/Time-of-Flight Mass Spectrometry. Rapid Commun. Mass Spectrom. 22 (2008) 1933-1940
27. Xu H., Zhang L., and Freitas M.A. Identification and Characterization of Disulfide Bonds in Proteins and Peptides from Tandem MS Data by Use of the MassMatrix MS/MS Search Engine. J. Proteome Res. 7 (2008) 138-144
28. Happersberger H.P., Bantscheff M., Barbirz S., and Glocker M.O. Multiple and Subsequent MALDI-MS On-Target Chemical Reactions for the Characterization of Disulfide Bonds and Primary Structures of Proteins. Methods Mol. Biol. 146 (2000) 167-184
29. Spiess C., Happersberger H.P., Glocker M.O., Spiess E., Rippe K., and Ehrmann M. Biochemical Characterization and Mass Spectrometric Disulfide Bond Mapping of Periplasmic α-Amylase MalS of Escherichia coli. J. Biol. Chem. 272 (1997) 22125-22133
30. Beavis R.C., and Chait B.T. Cinnamic Acid Derivatives as Matrices for Ultraviolet Laser Desorption Mass Spectrometry of Proteins. Rapid Commun. Mass Spectrom. 3 (1989) 432-435
31. Hutchens T.W., Nelson R.W., Li C.M., and Yip T.T. Synthetic Metal-Binding Protein Surface Domains for Metal Ion-Dependent Interaction Chromatography. I. Analysis of Bound Metal Ions by Matrix-Assisted UV Laser Desorption Time-of-Flight Mass Spectrometry. J. Chromatogr. A 604 (1992) 125-132
32. Huth-Fehre T., Gosine J.N., Wu K.J., and Becker C.H. Matrix-Assisted Laser Desorption Mass Spectrometry of Oligodeoxythymidylic Acids. Rapid Commun. Mass Spectrom. 6 (1992) 209-213
33. Hamdan M., Bordini E., Galvani M., and Righetti P.G. Protein Alkylation by Acrylamide, Its N-Substituted Derivatives and Cross-Linkers, and Its Relevance to Proteomics: A Matrix Assisted Laser Desorption/Ionization-Time of Flight-Mass Spectrometry Study. Electrophoresis 22 (2001) 1633-1644
34. Bordini E., Hamdan M., and Righetti P.G. Probing Acrylamide Alkylation Sites in Cysteine-Free Proteins by Matrix-Assisted Laser Desorption/Ionization Time-of-Flight. Rapid Commun. Mass Spectrom. 14 (2000) 840-848
35. Friedman M., Cavins J.F., and Wall J.S. Specific Modification of Protein Sulfhydryl Groups with α-, β-Unsaturated Compounds. J. Am. Chem. Soc. 87 (1965) 3672-3682
36. Chiari M., Righetti P.G., Negri A., Ceciliani F., and Ronchi S. Preincubation with Cysteine Prevents Modification of Sulfhydryl Groups in Proteins by Unreacted Acrylamide in a Gel. Electrophoresis 13 (1992) 882-884
37. Bordini E., Hamdan M., and Righetti P.G. Probing the Reactivity of S-S Bridges to Acrylamide in Some Proteins Under High pH Conditions by Matrix-Assisted Laser Desorption/Ionization. Rapid Commun. Mass Spectrom. 13 (1999) 1818-1827
38. Hunter E.P.L., and Lias S.G. Evaluated Gas Phase Basicities and Proton Affinities of Molecules: An Update. J. Phys. Chem. Ref. Data. 27 (1998) 413-656