Synthesis and solution structure of the antimicrobial peptide protegrin-1

European Journal of Biochemistry

Volumn 237, Issue 3, 1996, Pages 575-583

  Aumelas, André ^a   Mangoni, Mattéo ^b   Roumestand, Christian ^a   Chiche, Laurent ^a   Despaux, Ernest ^c   Grassy, Gérard ^a   Calas, Bernard ^b   Chavanieu, Alain ^b  

^a CENTRE DE BIOCHIMIE STRUCTURALE   (France)

^b Centre National de la Recherche Scientifique   (France)

^c MONTPELLIER UNIVERSITY HOSPITAL   (France)

Author keywords

Antimicrobial; Conformation; Disulfide bond; NMR; Protegrin

Indexed keywords

ANTIBIOTIC PROTEIN; ANTIINFECTIVE AGENT; PROTEGRIN 1; UNCLASSIFIED DRUG;

ANTIBACTERIAL ACTIVITY; ARTICLE; DRUG STRUCTURE; DRUG SYNTHESIS; ESCHERICHIA COLI; GRAM NEGATIVE BACTERIUM; GRAM POSITIVE BACTERIUM; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; STAPHYLOCOCCUS AUREUS; STAPHYLOCOCCUS EPIDERMIDIS;

EID: 0029886161     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0575p.x     Document Type: Article

References (53)

1. Bax, A. & Davis, D. G. (1985a) MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy, J. Magn. Reson. 65, 355-360.
2. Bax, A. & Davis, D. G. (1985b) Practical aspects of two-dimensional transverse NOE spectroscopy, J. Magn. Reson. 63, 207-213.
3. Bevins, C. L. (1994) Antimicrobial peptides as agents of mucosal immunity, Ciba Found. Symp. 186, 250-269.
4. 3, where X stands for one of the 20 common amino acids, J. Magn. Reson. 18, 191-198.
5. Cornet, B., Bonmatin, J. M., Hetru, C., Hoffmann, J. A., Ptak, M. & Vovelle F. (1995) Refined three-dimensional solution structure of insect defensin A, Structure 3, 435-448.
6. Dezheng, Z., Fujiwara, T. & Nagayama, K. (1989) Suppression of off-resonance effects in 1D and 2D ROESY, J. Magn. Reson. 81, 628-630.
7. Fujii, G., Selsted, M. E. & Eisenberg, D. (1993) Defensins promote fusion and lysis of negatively charged membranes, Protein Sci. 2, 1301-1312.
8. Gonnella, N. C., Zhang, X., Jin, Y., Prakash, O., Paris, C. G., Kolossvary, I., Guida, W. C., Bohacek, R. S., Vlattas, I. & Sytwu, T. (1994) Solvent effects on the conformation of cyclo(-D-Trp-D-Asp-Pro-D-Val-Leu-). An NMR spectroscopy and molecular modelling study, Int. J. Pept. Protein Res. 43, 454-462.
9. Guenot, J. M. & Kollman, P. A. (1992) Molecular dynamics studies of a DNA-binding protein, Protein Sci. 1, 1185-1205.
10. Günther, P., Braun, W. & Wüthrich, K. (1991) Efficient computation of three-dimensional protein structures in solution from NMR data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA, J. Mol. Biol. 217, 517-530.
11. Hanzawa, H., Shimada, I., Kuzuhara, T., Komano, H., Kohda, D., Inagaki, F., Natori, S. & Arata, Y. (1990) 1H nuclear magnetic resonance study of the solution conformation of an antibacterial protein, sapecin, FEBS Lett. 269, 413-420.
12. Harwig, S., Swiderek, K., Lee, T. & Lehrer, R. (1995) Determination of disulphide bridges in protegrin-2, an antimicrobial peptide from porcine leukocytes, J. Pept. Sci. 3, 207-215.
13. Hurle, M. R., Eads, C. D., Pearlman, D. A., Seibel, G. L., Thomason, J., Kosen, P. A., Kollman, P. A., Anderson, S. & Kuntz, I. D. (1992) Comparison of solution structures of mutant bovine pancreatic trypsin inhibitor proteins using two-dimensional nuclear magnetic resonance, Protein Sci. 1, 91-106.
14. Kawano, K., Yoneya, T., Miyata, T., Yoshikawa, K., Tokunaga, F., Terada, Y. & Iwanaga, S. (1990) Antimicrobial peptide, tachyplesin I, isolated from hemocytes of the horseshoe crab (Tachypleus tridentatus). J. Biol. Chem. 265, 15365-15367.
15. Kini, M. R. & Evans, H. J. (1989) A common cytolytic region in myotoxins, hemolysins, cardiotoxins and antibacterial peptides, Int. J. Pept. Protein Res. 34, 277-286.
16. Kokryakov, V. N., Harwig, S. S. L., Panyutich, E. A., Shevchenko, A. A., Aleshina, G. M., Shamova, O. V., Korneva, H. A. & Lehrer, R. (1993) Protegrins: leukocyte antimicrobial peptides that combine features of corticostatic defensins and tachyplesins, FEBS Lett. 327, 231-236.
17. Kyte, J. & Doolittle, R. F. (1982) A simple method for displaying the hydrophobic character of a protein, J. Mol. Biol. 157, 105-132.
18. 13C NMR chemical shifts and the secondary and tertiary structure of a zinc finger peptide, J. Biomol. NMR 2, 307-322.
19. Lippens, G., Dhalluin, C. & Wieruszeski, J. M. (1995) Use of the water flip-back pulse in the homonuclear NOESY experiment, J. Biomol. NMR 5, 327-331.
20. Macura, S., Huang, Y., Sutter, D. & Ernst, R. R. (1981) Two-dimensional chemical exchange and cross relaxation spectroscopy of coupled nuclear spins, J. Magn. Reson. 43, 259-281.
21. Maloy, W. L. & Kari, U. P. (1995) Structure-activity studies on magainins and other host defense peptides, Biopolymers 37, 105-122.
22. Marion, D., Ikura, M., Tschudin, R. & Bax, A. (1989) Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins, J. Magn. Reson. 85, 393-399.
23. Matsuzaki, K., Fukui, M., Fujii, N. & Miyajima, K. (1991) Interactions of an antimicrobial peptide, tachyplesin I, with lipid membrane, Biochim. Biophys. Acta 1070, 259-264.
24. Matsuzaki, K., Nakayama, M., Fukui, M., Otaka, A., Funakoshi, S., Fujii, N., Bessho, K. & Miyajima, K. (1993) Role of disulfide linkages in tachyplesin-lipid interactions, Biochemistry 32, 11704-11710.
25. Migorodskaya, O. A., Shevchenko, A. A., Abdalla, K. O., Chernushevich, I. V., Egorov, T. A., Musoliamov, A. X., Kokryakov, V. N. & Shamova, O. V. (1993) Primary structure of three cationic peptides from porcine neutrophils, FEBS Lett. 330, 339-342.
26. Miyata, T., Tokunaga, F., Yoneya, T., Yoshikawa, K., Iwanaga, S., Niwa, M., Takao, T. & Shimonishi, Y. (1989) Antimicrobial peptides, isolated from horseshoe crab hemocytes, tachyplesin II, and polyphemusins I and II: chemical structures and biological activity, J. Biochem. (Tokyo) 106, 663-668.
27. Nakamura, T., Furanaka, H., Miyata, T., Tokunaga, F., Muta, T., Iwanaga, S., Niwa, M., Takao, T. & Shimonishi, Y. (1988) Tachyplesin, a class of antimicrobial peptides from the hemocytes of the horseshoe crab (Tachypleus tridentatus). Isolation and chemical structure, J. Biol. Chem. 263, 16709-16713.
28. Park, N. G., Lee, S., Oishi, O., Aoyagi, H., Iwanaga, S., Yamashita, S. & Ohno, M. (1992) Conformation of tachyplesin I from Tachypleus tridentatus when interacting with lipid matrices, Biochemistry 31, 12241-12247.
29. Pearlman, D. A., Case, D. A., Caldwell, J. C., Ross, W. S., Cheatham, T. E., Ferguson, D. M., Seibel, G. L., Chandra Singh, U., Weiner, P. & Kollman, P. A. (1995) AMBER 4.1, University of California, San Francisco.
30. Piotto, M., Saudek, V. & Sklenar, V. (1992) Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions, J. Biomol. NMR 2, 661-665.
31. Rance, M., Sorensen, O. W., Bodenhausen, G., Wagner, G., Ernst, R. R. & Wüthrich, K. (1983) Improved spectral resolution in COSY 1H NMR spectra of proteins via double quantum filtering, Biochem. Biophys. Res. Commun. 117, 479-485.
32. Rance, M. (1987) Improved techniques for homonuclear rotating-frame and isotropic mixing experiments, J. Magn. Reson. 74, 557-564.
33. Romeo, D., Skerlavaj, B., Bolognesi, M. & Gennaro, R. (1988) Structural and bactericidal activity of an antibiotic dodecapeptide purified from bovine neutrophils, J. Biol. Chem. 263, 9573-9575.
34. Roumestand, C., Mispelter, J., Austruy, C. & Canet, D. (1995) The use of band-filtering in multidimensinal NMR. Evaluation of two 'user-friendly' techniques, J. Magn. Reson. B109, 153-164.
35. Selsted, M. E. & Ouelette, A. J. (1995) Defensins in granules of phagocytic and non-phagocytic cells, Trends Cell Biol. 5, 114.
36. Smith, J. A. & Pease, L. G. (1980) Reverse turns in peptides and proteins, CRC Crit. Rev. Biochem. 8, 315-399.
37. Tam, J., Wu, C., Liu, W. & Zhang, J. (1991) Disulfide bond formation in peptides by dimethyl sulfoxide. Scope and applications, J. Am. Chem. Soc. 113, 6657-6662.
38. Tamamura, H., Kuroda, M., Masuda, M., Otaka, A., Funakoshi, S., Nakashima, H., Yamamoto, N., Waki, M., Matsumoo, A., Lancellin, J. M., Kohda, D., Tate, S., Inagaki, F. & Fujii, N. (1993) A comparative study of the solution structures of tachyplesin I and a novel anti HIV synthetic peptide, T22([Tyr5,12, Lys7]-polyphemusin H), determined by nuclear magnetic resonance, Biochim. Biophys. Acta 1163, 209-216.
39. Vaara, M. (1992) Agents that increase the permeability of the outer membrane, Microbiol. Rev. 56, 395-411.
40. Vaisman, I. I. & Berkovitz, M. L. (1992) Local structural order and molecular associations in water-DMSO mixtures. Molecular dynamics study, J. Am. Chem. Soc. 114, 7889.
41. van Gunsteren, W. F. & Berendsen, H. J. C. (1977) Algorithms for macromolecular dynamics and constraints dynamics, Mol. Phys. 34, 1311-1327.
42. Weiner, S. J., Kollman, P. A., Le-Nguyen, D. T. & Case, D. A. (1986) An all atom force field for simulation of proteins and nucleic acids, J. Comput. Chem. 7, 230-252.
43. White, S. H., Wimley, W. & Selsted, M. E. (1995) Structure, function, and membrane integration of defensins, Curr. Opin. Struct. Biol. 5, 521-527.
44. Wishart, D. S., Sykes, B. D. & Richards, F. M. (1991) Relationship between nuclear magnetic resonance chemical shift and protein secondary structure, J. Mol. Biol. 222, 311-333.
45. Wishart, D. S. & Sykes, B. D. (1994) Chemical shifts as a tool for structure determination in Methods Enzymol. 239, 363-392.
46. 15N random coil NMR chemical shifts of the common amino acids. Investigation of the nearest-neighbour effect, J. Biol. NMR 5, 67-81.
47. Wimley, W. C., Selsted, M. E. & White, S. H. (1994) Interactions between human defensins and lipid bilayers: evidence for formation of multimeric pores, Protein Sci. 3, 1362-1373.
48. 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.
49. Wüthrich, K. (1986) NMR of proteins & nucleic acids, John Wiley & Sons, New York.
50. Zhao, C., Liu, L. & Lehrer, R. (1994) Identification of a new member of the protegrin family by cDNA cloning, FEBS Lett. 346, 285-288.
51. Zhao, C., Ganz, T. & Lehrer, R. (1995) The structure of porcine genes, FEBS Lett. 368, 197-202.
52. Zhu, Q., Hu, J., Mulay, S., Esch, F., Shimasaki, S. & Solomon, S. (1988) Isolation and structure of corticostatin peptides from rabbit fetal and adult lung, Proc. Natl Acad. Sci. USA 85, 592-596.
53. Zimmermann, G. R., Legault, P., Selsted, M. E. & Pardi, A. (1995) Solution structure of bovine neutrophil β-defensin-12: the peptide fold of the β-defensins is identical to that of the classical defensins, Biochemistry 34, 13663-13671.