NMR structural characterization of cecropin A(1-8) - magainin 2(1-12) and cecropin A(1-8) - melittin(1-12) hybrid peptides

Journal of Peptide Research

Volumn 53, Issue 5, 1999, Pages 578-589

  Oh, D ^a   Shin, S Y ^b   Kang, J H ^b   Hahm, K S ^b   Kim, K L ^b   Kim, Y ^a  

^a Konkuk University   (South Korea)

^b Korea Institute of Science and Technology   (South Korea)

Author keywords

CA(1 8) ME(1 12); CA(1 8) MA(1 12); Hemolytic activity; NMR spectroscopy; Tertiary structure

Indexed keywords

CECROPIN; CECROPIN A; MAGAININ 2;

ANTIMICROBIAL ACTIVITY; ARTICLE; DRUG STRUCTURE; HYDROPHOBICITY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN STRUCTURE; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; ANTI-BACTERIAL AGENTS; ANTIMICROBIAL CATIONIC PEPTIDES; CARCINOMA, SMALL CELL; CIRCULAR DICHROISM; ERYTHROCYTES; HEMOLYSIN PROTEINS; HUMANS; LUNG NEOPLASMS; MAGNETIC RESONANCE SPECTROSCOPY; MELITTEN; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN CONFORMATION; STRUCTURE-ACTIVITY RELATIONSHIP; TUMOR CELLS, CULTURED;

EID: 0033061716     PISSN: 1397002X     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1399-3011.1999.00067.x     Document Type: Article

References (41)

1. Boman, H.G. & Hultmark, D. (1987) Cell-free imunity in insects. Annu. Rev. Microbiol. 41, 103-126.
2. Steiner, H., Andreu, D. & Merrifield, R.B. (1988) Binding and action of cecropin and cecropin analogues: antibacterial peptides from insects. Biochim. Biophys. Acta. 939, 260-266.
3. Habermann, E. & Jentsch, J. (1967) Sequence analysis of melittin from tryptic and peptic degradation products. Hoppe Seylers Z. Physiol. Chem. 348, 37-50.
4. Blondelle, S.E., Simpkins, L.R., Pérez-Payá, E. & Houghten, R.A. (1993) Influence of tryptophan residues on melittin's hemolytic activity. Biochim. Biophys. Acta. 1202, 331-336.
5. Zasloff, M. (1987) Magainins, a class antimicrobial peptides from Xenopus skin: isolation, characterization of two active form, and partial cDNA sequence of a precursor. Proc. Natl Acad. Sci. USA 84, 5449-5453.
6. Soravia, E., Martini, G. & Zasloff, M. (1988) Antimicrobial properties of peptides from Xenopus granular gland secretions. FEBS Lett. 228, 337-340.
7. Boman, H.G., Wade, D., Boman, A., Wahlin, B. & Meriffield, R.B. (1989) Antibacterial and antimalarial properties of peptides that are cecropin-melittin hybrids. FEBS Lett. 259, 103-106.
8. Andreu, D., Ubach, J., Boman, A., Wahlin, B., Wade, D., Merrifield, R.B. & Boman, H.G. (1992) Shortened cecropin A-melittin hybrids: significant size reduction retains potent antibiotic activity. FEBS Lett. 296, 190-194.
9. Wade, D., Andreu, D., Mitchell, S.A., Silveira, A.M., Boman, A., Boman, H.G. & Merrifield, R.B. (1992) Antibacterial peptides designed as analogs or hybrids of cecropins and melittin. Int. J. Peptide Protein Res. 40, 429-436.
10. Diaz-Achirica, P., Ubach, J., Guinea, A., Andreu, D. & Rivas, L. (1998) The plasma membrane of Leishmania donovani promastigotes is the main target for CA(1 8)-M(1-18), a synthetic cecropin A-melittin hybrid peptide. Biochem. J. 330, 453-460.
11. Fernández, I., Ubach, J., Reig, F., Andreu, D. & Pons, M. (1994) Effect of succinylation on the membrane activity and conformation of a short cecropin A-melittin hybrid peptide. Biopolymers 34, 1251-1258.
12. Mancheno, J.M., Onaderra, M., Martínez del Pozo, A., Díaz-Achirica, P., Andreu, D., Rivas, L. & Gavilanes, J.G. (1996) Release of lipid vesicle contents by an antibacterial cecropin A-melittin hybrid peptide. Biochemistry 35, 9892-9899.
13. Fernández, I., Ubach, J., Andreu, D. & Pons, M. (1996) NMR characterization of self-association of a helical peptide using deuterium exchange experiments. Colloids Surf. 115, 39-45.
14. Sipos, D., Chandrasckhar, K., Arvidsson K. & Engström. & Ehrenberg, A. (1991) Two-dimensional proton-NMR studies on a hybrid peptide between cecropin A and melittin. Eur. J. Biochem. 199, 285-291.
15. Shin, S.Y., Lee, M.K., Kim, K.L. & Hahm, K.-S. (1997) Structure-antitumor and hemolytic activity cecropin A-magainin 2 and cecropin A-melittin hybrid peptides. J. Peptide Res. 50, 279-285.
16. Chen, Y.-H., Yang, J.T. & Chau, K.H, (1974) Determination of the helix and β form of proteins in aqueous solution by circular dichroism. Biochemistry 11, 4120-4131.
17. Derome, A. & Williamson, M. (1990) Rapid-pulsing artifacts in double-quantum-filtered COSY J. Magn. Reson. 88, 177-185.
18. Bax, A. & Davis, D.G. (1985) MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65, 355-360.
19. Macura, S. & Ernst, R.R. (1980) Elucidation of cross-relaxation in liquids by two-dimensional NMR spectroscopy. Mol. Phys. 41, 95-117.
20. Bax, A. & Davis, D.G. (1985) Practical aspects of two-dimensional transverse NOE spectroscopy. J. Magn. Reson. 63, 207-213.
21. 1H spin-spin coupling constants in proteins. Biochem. Biophys. Res. Commun. 113, 967-974.
22. Muller, L. (1987) P.E.COSY, a simple alternative to E.COSY. J. Magn. Reson. 72, 191-197.
23. Molecular Simulations Inc. San Diego, CA, USA.
24. Clore, G.M. & Gronenborn, A.M. (1989) Determination of three-dimensional structures of proteins and nucleic acids in solution by nuclear magnetic resonance spectroscopy. CRC Crit. Rev. Biochem. Mol. Biol. 24, 479-564.
25. Clore, G.M. & Gronenborn, A.M. (1994) Structures of larger proteins, protein-ligand and protein DNA complexes by multidimensional heteronuclear NMR. Protein Sci. 3, 372-390.
26. Brünger, A.T. (1993) x-plor Manual, Version 3.1. Yale University, New Haven, CT.
27. Wüthrich, K., Billeter, M. & Braun, W. (1983) Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance. J. Mol. Biol. 169, 949-961.
28. Clore, G.M., Gronenborn, A.M., Nilges, M. & Ryan, C.A. (1987) Three-dimensional structure of potato carboxypeptidase inhibitor in solution. A study using nuclear magnetic resonance, distance geometry, and restrained molecular dynamics. Biochemistry 26, 8012-8023.
29. Nilges, M., Clore, G.M. & Gronenborn, A.M. (1988) Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations. FEBS Lett. 229, 317-324.
30. Kuszewski, J., Nilges, M. & Brünger, A.T. (1992) Sampling and efficiency of metric matrix distance geometry: a novel partial metrization algorithm. J. Biomol. NMR 2, 33-56.
31. Wüthrich, K. (1986) In NMR of Protein and Nucleic Acid. John Wiley & Sons, New York.
32. Wishart, D.S., Sykes, B.D. & Richards, F.M. (1992) The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31, 1647-1651.
33. Kim, Y. & Prestegard, J.H. (1989) Measurement of vicinal couplings from cross peaks in COSY spectra. J. Magn. Reson. 84, 9-13.
34. Holak, T.A., Engström, A., Kraulis, P.J., Lindeberg, G., Bennich, H., Jones, T.A., Gronenborn, A.M. & Clore, G.M. (1988) The solution conformation of the antibacterial peptide cecropin A: a nuclear magnetic resonance and dynamical simulated annealing study. Biochemistry 27, 7620-7629.
35. Sipos, D., Andersson, M. & Ehrenberg, A. (1992) The structure of the mammanlian antibacterial peptide cecropin P1 in solution, determined by proton-NMR Eur. J. Biochem. 209, 163-169.
36. 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an α-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution. J. Biomol. NMR 9, 127-135.
37. 1H-NMR study in methanol. Eur. J. Biochem. 173, 139-146.
38. Ikura, T., Go, N. & Inagaki, F. (1991) Refined structure of melittin bound to perdeuterated dodecylphosphocholine micelles as studied by 2D-NMR and distance geometry calculation. Proteins: Struct. Funct. Genet. 9, 81-89.
39. Shai, Y., Bach, D. & Yanovsky, A. (1990) Channel formation properties of synthetic peptides of pardaxin analogues. J. Biol. Chem. 265, 20202-20209.
40. Fink, J., Boman, A., Boman, H.G. & Merrifield, R.B. (1989) Design, synthesis and antibacterial activity of cecropin-like model peptides. Int. J. Peptide Protein Res. 33, 412-421.
41. Shin, S.Y., Kang, J.H., Lee, M.K., Kim, S.Y., Kim, Y. & Hahm, K.-S. (1998) Cecropin A-magainin 2 hybrid peptides having potent antimicrobial activity with low hemolytic effect. Biochem. Mol. Biol. Int. 44, 1119-1126.