Solution structure of the antimicrobial peptide gaegurin 4 by 1H and 15N nuclear magnetic resonance spectroscopy

European Journal of Biochemistry

Volumn 267, Issue 9, 2000, Pages 2695-2704

  Park, Sang Ho ^a   Kim, Yun Kyong ^a   Park, Jung Won ^b   Lee, ByeongJae ^b   Lee, Bong Jin ^a  

^a Department of Pharmacy ^*  (South Korea)

^b Seoul National University   (South Korea)

Author keywords

Antimicrobial peptide; GGN4; NMR; Solution structure; helix

Indexed keywords

CYSTEINE; DISULFIDE; DODECYL SULFATE SODIUM; GAEGURIN; PHOSPHORYLCHOLINE; POLYPEPTIDE ANTIBIOTIC AGENT; TRIFLUOROETHANOL; UNCLASSIFIED DRUG; WATER;

ALPHA HELIX; ANIMAL TISSUE; ANTIMICROBIAL ACTIVITY; AQUEOUS SOLUTION; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; DISULFIDE BOND; FROG; MASS SPECTROMETRY; MICELLE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN ISOLATION; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; SKIN;

AMINO ACID SEQUENCE; ANTI-BACTERIAL AGENTS; CIRCULAR DICHROISM; DISULFIDES; MAGNETIC RESONANCE SPECTROSCOPY; MICROBIAL SENSITIVITY TESTS; MOLECULAR SEQUENCE DATA; NITROGEN ISOTOPES; PEPTIDES; PROTEIN PRECURSORS; PROTEIN STRUCTURE, SECONDARY; PROTONS; SOLUTIONS;

ANIMALIA; ANURA; PROKARYOTA; RANA RUGOSA;

EID: 0000953014     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.01287.x     Document Type: Article

References (52)

1. 1. Gabay, J.E. (1994) Ubiquitous natural antibiotics. Science 264, 373-374.
2. 2. Nicolas, P. & Mor, A. (1995) Peptides as weapons against microorganisms in the chemical defense system of vertebrates. Annu. Rev. Microbial. 49, 277-304.
3. 3. Boman, H.G. (1995) Peptide antibiotics and their role in innate immunity. Annu. Rev. Immunol. 13, 61-92.
4. 4. Zasloff, M. (1987) Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc. Natl Acad. Sci. USA 84, 5449-5453.
5. 5. Morikawa, N., Hagiwara, K. & Nakajima, T. (1992) Brevinin-1 and -2, unique antimicrobial peptides from the skin of the frog, Rana brevipoda porsa. Biochem. Biophys. Res. Commun. 189, 148-190.
6. 6. Simmaco, M., Mignogna, G., Barra, D. & Bossa, F. (1993) Novel antimicrobial peptides from skin secretion of the European frog Rana esculenta. FEBS Lett. 324, 159-161.
7. 7. Clark, D.P., Durell, S., Maloy, W.L. & Zasloff, M. (1994) Ranalexin. A novel antimicrobial peptide from bullfrog (Rana catesbeiana) skin, structurally related to the bacterial antibiotic, polymyxin. J. Biol. Chem. 269, 10849-10855.
8. 8. Mor, A., Nguyen, V.H., Delfour, A., Migliore-Samour, D. & Nicolas, P. (1991) Isolation, amino acid sequence, and synthesis of dermaseptin, a novel antimicrobial peptide of amphibian skin. Biochemistry 30, 8824-8830.
9. 9. Gibson, B.W., Tang, D.Z., Mandrell, R., Kelly, M. & Spindel, E.R. (1991) Bombinin-like peptides with antimicrobial activity from skin secretions of the Asian toad Bombina orientalis. J. Biol. Chem. 266, 23103-23111.
10. 10. Simmaco, M., Barra, D., Chiarini, F., Noviello, L., Melchiorri, P., Kreil, G. & Richter, K. (1991) A family of bombinin-related peptides from the skin of Bombina variegata. Eur. J. Biochem. 199, 217-222.
11. 11. Park, J.M., Jung. J.E. & Lee, B.J. (1994) Antimicrobial peptides from the skin of a Korean frog, Rana rugosa. Biochem. Biophys. Res. Commun. 205, 948-954.
12. 12. Park, J.M., Lee, J.Y., Moon, H.M. & Lee, B.J. (1995) Molecular cloning of cDNAs encoding precursors of frog skin antimicrobial peptides from Rana rugosa. Biochim. Biophys. Acta 1264, 23-25.
13. 13. Marion, D., Zasloff, M. & Bax, A. (1988) A two-dimensional NMR study of the antimicrobial peptide magainin 2. FEBS Lett. 227, 21-26.
14. 14. Bechinger, B., Zasloff, M. & Opella, S.J. (1992) Structure and interactions of magainin antibiotic peptides in lipid bilayers: a solid-state nuclear magnetic resonance investigation. Biophys. J. 62, 12-24.
15. 15. Bechinger, B., Zasloff, M. & Opella, S.J. (1993) Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy. Protein Sci. 12, 2077-2084.
16. 16. Bechinger, B., Gierasch, L.M., Montal, M., Zasloff, M. & Opella, S.J. (1996) Orientations of helical peptides in membrane bilayers by solid state NMR spectroscopy. Solid State Nucl. Magn. Reson. 3, 185-191.
17. 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an alpha-helix in dodecylphosphocholine micelles, sodium dodecyl-sulfate micelles, and trifluoroethanol/water solution. J. Biomol. NMR 2, 127-135.
18. 18. Bechinger, B., Zasloff, M. & Opella, S.J. (1998) Structure and dynamics of the antibiotic peptide PGLa in membranes by solution and solid-state nuclear magnetic resonance spectroscopy. Biophys. J. 74, 981-987.
19. 19. Maloy, W.L. & Kari, U.P. (1995) Structure-activity studies on magainins and other host defense peptides. Biopolymers (Peptide Sci.) 37, 105-122.
20. 20. Kwon, M.Y., Hong, S.Y. & Lee, K.H. (1998) Structure-activity analysis of brevinin 1E amide, an antimicrobial peptide from Rana esculenta. Biochim. Biophys. Acta 1387, 239-248.
21. 21. Vignal, E., Chavanieu, A., Roch, P., Chiche, L., Grassy, G., Calas, B. & Aumelas, A. (1998) Solution structure of the antimicrobial peptide ranalexin and a study of its interaction with perdeuterated dodecylphosphocholine micelles. Eur. J. Biochem. 253, 221-228.
22. 22. Kim, H.J., Han, S.K., Park, J.B., Baek, H.J., Lee, B.J. & Ryu, P.D. (1999) Gaegurin 4, a peptide antibiotic of frog skin, forms voltage-dependent channels in planar lipid bilayers. J. Pept. Res. 53, 1-7.
23. 23. Kim, S.H., Kim, J.Y., Lee, B.J. & Kim, S.J. (1999) Synthesis and characterization of GGN4 and its tryptophan substitued analogue peptides. J. Biochem. Mol. Biol. 32, 12-19.
24. 24. Kim, J., Park, J.M. & Lee, B.J. (1997) High-level expression and efficient purification of the antimicrobial peptide gaegurin 4 in E. coli. Proteins Peptide Lett. 4, 391-396.
25. 25. 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.
26. 26. Greenfield, N. & Fasman, G.D. (1969) Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 8, 108-116.
27. 15N-labeled proteins. J. Magn. Reson. 86, 110-126.
28. 28. Delaglio, F., Grzesiek, S., Vuister, G., Zhu, G., Pfeifer, J. & Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293.
29. 29. Wüthirch, K., Billerter, 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.
30. 30. Nilges, M., Gronenborn, A.M., Brünger, A.T. & Clore, G.M. (1988) Determination of three-dimensional structures of proteins by simulated annealing with interproton distance restraints. Application to crambin, potato carboxypeptidase inhibitor and barley serine proteinase inhibitor 2. Protein Eng. 2, 27-38.
31. 31. Brünger, A.T. (1992) XPLOR 3.1. A System for X-Ray Crystallography and NMK. Yale University Press, New Haven.
32. 32. Wüthrich, K. (1986) NMR of Proteins, and Nucleic Acids. Wiley, New York.
33. 33. Wishart, D.S., Sykes, B.D. & Richards, P.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.
34. 1H chemical shfits obtained as a function of temperature and trifluoroethanol concentration for the peptide sereis GGXGG. J. Biomol. NMR 5, 14-24.
35. 35. Segawa, S., Fukuno, T., Fujiwara, K. & Noda, Y. (1991) Local structures in unfolded lysozyme and correlation with secondary structures in the native conformation: helix-forming or -breaking propensity of peptide segments. Bioploymers 31, 497-509.
36. 36. Dyson, H.J., Merutka, G., Waltho, J.P., Lerner, R.A. & Wright, P.E. (1992) Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Myohemerythrin. J. Mol. Biol. 226, 795-817.
37. 37. Sönnichsen, F.D., Van Eyk, J.E., Hodges, R.S. & Sykes, B.D. (1992) Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide. Biochemistry 31, 8790-8798.
38. 38. Shon, K.J., Kim, Y., Colnago, L.A. & Opella, S.J. (1991) NMR studies of the structure and dynamics of membrane-bound bacteriophage Pf1 coat protein. Science 252, 1303-1305.
39. 39. McDonnell, P.A., Shon, K., Kim, Y. & Opella, S.J. (1993) fd coat protein structure in membrane environments. J. Mol. Biol. 233, 447-463.
40. 40. Papavoine, C.H., Aelen, J.M., Konings, R.N., Hilbers, C.W. & Van de Ven, F.J. (1995) NMR studies of the major coat protein of bacteriophage M13. Structural information of gVIIIp in dodecylphosphocholine micelles. Eur. J. Biochem. 232, 490-500.
41. 15N nuclear magnetic resonance relaxation measurements using the model-free approach and reduced spectral density mapping. Biochemistry 36, 4015-4026.
42. 42. Almeida, F.C. & Opella, S.J. (1997) fd coat protein structure in membrane environments: structural dynamics of the loop between the hydrophobic trans-membrane helix and the amphipathic in-plane helix. J. Mol. Biol. 270, 481-495.
43. 43. Nambudripad, R., Stark, W., Opella, S.J. & Makowski, L. (1991) Membrane-mediated assembly of filamentous bacteriophage Pf1 coat protein. Science 252, 1305-1308.
44. 44. Papavoine, C.H., Christiaans, B.E., Folmer, R.H., Konings, R.N. & Hilbers, C.W. (1998) Solution structure of the M13 major coat protein in detergent micelles: a basis for a model of phage assembly involving specific residues. J. Mol. Biol. 282, 401-419.
45. 45. Steiner, H., Hultmark, D., Engström, A., Bennich, H. & Boman, H.G. (1981) Sequence and specificity of two antimicrobial proteins involved in insect immunity. Nature 292, 246-248.
46. 46. 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.
47. 47. Gazit, E., Lee, W.J., Brey, P.T. & Shai, Y. (1994) Mode of action of the antibacterial cecropin B2: a spectrofluorometric study. Biochemistry 33, 10681-10692.
48. 48. Gazit, E., Boman, A., Boman, H.G. & Shai, Y. (1995) Interaction of the mammalian antibacterial peptide cecropin P1 with phospholipid vesicles. Biochemistry 34, 11479-11488.
49. 49. Gazit, E., Miller, I.R., Biggin, P.C., Sansom, M.S. & Shai, Y. (1996) Structure and orientation of the mammalian antibacterial peptide cecropin P1 within phospholipid membranes. J. Mol. Biol. 258, 860-870.
50. 50. Christensen, B., Fink, J., Merrifield, R.B. & Mauzerall, D. (1988) Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes. Proc. Natl Acad. Sci. USA 85, 5072-5076.
51. 51. Sun, J.Y., Lee, K.H., Chi, S.W., Hong, S.Y., Choi, B.W., Moon, H.M. & Choi, B.S. (1996) Unusually stable helical kink in the antimicrobial peptide - a derivative of gaegurin. FEBS Lett. 392, 309-312.
52. 52. Kyte, J. & Doolittle, R.F. (1982) A simple method for displaying the hydrophobic character of a protein. J. Mol. Biol. 157, 105-132.