Determination of disulfide linkages in antimicrobial peptides of the macin family by combination of top-down and bottom-up proteomics

Journal of Proteomics

Volumn 103, Issue , 2014, Pages 216-226

  Hung, Chien Wen ^a   Jung, Sascha ^a   Grötzinger, Joachim ^a   Gelhaus, Christoph ^a   Leippe, Matthias ^a   Tholey, Andreas ^a  

^a UNIVERSITY OF KIEL   (Germany)

Author keywords

Cleavage site; De novo Sequencing; LC MS; Posttranslational modification; Top down

Indexed keywords

CYSTEINE; DISULFIDE; HYDRAMACIN 1; MACIN; NEUROMACIN; POLYPEPTIDE ANTIBIOTIC AGENT; THEROMACIN; UNCLASSIFIED DRUG; ANTIMICROBIAL CATIONIC PEPTIDE; HYDRAMACIN-1, HYDRA MAGNIPAPILLATA; NEUROMACIN PEPTIDE, HIRUDO MEDICINALIS; THEROMACIN, LEECH;

ARTICLE; DISULFIDE BOND; MOLECULAR WEIGHT; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CLEAVAGE; PROTEIN DEGRADATION; PROTEOMICS; SEQUENCE ANALYSIS; TANDEM MASS SPECTROMETRY; AMINO ACID SEQUENCE; CHEMISTRY; ISOLATION AND PURIFICATION; PROCEDURES; SEQUENCE ALIGNMENT;

AMINO ACID SEQUENCE; ANTIMICROBIAL CATIONIC PEPTIDES; DISULFIDES; MOLECULAR WEIGHT; PROTEOMICS; SEQUENCE ALIGNMENT; TANDEM MASS SPECTROMETRY;

EID: 84899766898     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2014.04.001     Document Type: Article

References (21)

1. Nakatsuji T., Gallo R.L. Antimicrobial peptides: old molecules with new ideas. J Invest Dermatol 2012, 132:887-895.
2. Wang G., Li X., Wang Z. APD2: the updated antimicrobial peptide database and its application in peptide design. Nucleic Acids Res 2009, 37:D933-D937.
3. Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 2002, 415:389-395.
4. Lai Y., Gallo R.L. AMPed up immunity: how antimicrobial peptides have multiple roles in immune defense. Trends Immunol 2009, 30:131-141.
5. Jung S., Dingley A.J., Augustin R., Anton-Erxleben F., Stanisak M., Gelhaus C., et al. Hydramacin-1, structure and antibacterial activity of a protein from the basal metazoan Hydra. J Biol Chem 2009, 284:1896-1905.
6. Jung S., Sönnichsen F.D., Hung C.W., Tholey A., Boidin-Wichlacz C., Haeusgen W., et al. Macin family of antimicrobial proteins combines antimicrobial and nerve repair activities. J Biol Chem 2012, 287:14246-14258.
7. Yano H., Kuroda S., Buchanan B.B. Disulfide proteome in the analysis of protein function and structure. Proteomics 2002, 2:1090-1096.
8. Zhang B., Cockrill S.L. Methodology for determining disulfide linkage patterns of closely spaced cysteine residues. Anal Chem 2009, 81:7314-7320.
9. Sanger F. A disulphide interchange reaction. Nature 1953, 171:1025-1026.
10. Brunger A.T. X-ray crystallography and NMR reveal complementary views of structure and dynamics. Nat Struct Biol 1997, 4(Suppl.):862-865.
11. Gorman J.J., Wallis T.P., Pitt J.J. Protein disulfide bond determination by mass spectrometry. Mass Spectrom Rev 2002, 21:183-216.
12. Mauri P., Toppo S., De Palma A., Benazzi L., Maiorino M., Ursini F. Identification by MS/MS of disulfides produced by a functional redox transition. Methods Enzymol 2010, 473:217-225.
13. Williamson R.A., Marston F.A., Angal S., Koklitis P., Panico M., Morris H.R., et al. Disulphide bond assignment in human tissue inhibitor of metalloproteinases (TIMP). Biochem J 1990, 268:267-274.
14. Tang Y.Q., Selsted M.E. Characterization of the disulfide motif in BNBD-12, an antimicrobial beta-defensin peptide from bovine neutrophils. J Biol Chem 1993, 268:6649-6653.
15. Jenspersen A.M., Christensen T., Klausen N.K., Nielsen P.F., Sorensen H.H. Characterisation of a trisulphide derivative of biosynthetic human growth hormone produced in Escherichia coli. Eur J Biochem 1994, 219:365-373.
16. Canova-Davis E., Baldonado I.P., Chloupek R.C., Ling V.T., Gehant R., Olson K., et al. Confirmation by mass spectrometry of a trisulfide variant in methionyl human growth hormone biosynthesized in Escherichia coli. Anal Chem 1996, 68:4044-4051.
17. Mormann M., Eble J., Schwoppe C., Mesters R.M., Berdel W.E., Peter-Katalinic J., et al. Fragmentation of intra-peptide and inter-peptide disulfide bonds of proteolytic peptides by nanoESI collision-induced dissociation. Anal Bioanal Chem 2008, 392:831-838.
18. Durand XM Kirt L., Plummer Chelsea E., Xia Yu Tandem mass spectrometry (MSn) of peptide disulfide regio-isomers via collision-induced dissociation: Utility and limits in disulfide bond characterization. Int J Mass Spectrom 2013, 343-344:50-57.
19. Wu S.L., Jiang H., Lu Q., Dai S., Hancock W.S., Karger B.L. Mass spectrometric determination of disulfide linkages in recombinant therapeutic proteins using online LC-MS with electron-transfer dissociation. Anal Chem 2009, 81:112-122.
20. Tsai Pei L., Chen S.-F., Huang Sheng Y. Mass spectrometry-based strategies for protein disulfide bond identification. Rev Anal Chem 2013, 32:257-294.
21. Echterbille J., Quinton L., Gilles N., De Pauw E. Ion mobility mass spectrometry as a potential tool to assign disulfide bonds arrangements in peptides with multiple disulfide bridges. Anal Chem 2013, 85:4405-4413.