A comparative study on the structure and function of a cytolytic α- helical peptide and its antimicrobial β-sheet diastereomer

European Journal of Biochemistry

Volumn 259, Issue 1-2, 1999, Pages 360-369

  Oren, Ziv ^a   Hong, Jiang ^a   Shai, Yechiel ^a  

^a WEIZMANN INSTITUTE OF SCIENCE   (Israel)

Author keywords

Antimicrobial; Cytotoxicity; Membrane; Peptide; Structure

Indexed keywords

POLYPEPTIDE ANTIBIOTIC AGENT;

ANTIBACTERIAL ACTIVITY; ARTICLE; CONTROLLED STUDY; DRUG CYTOTOXICITY; HEMOLYSIS; HUMAN; HUMAN CELL; HYDROPHOBICITY; INFRARED SPECTROSCOPY; NONHUMAN; PEPTIDE ANALYSIS; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN CONFORMATION;

AMINO ACID SEQUENCE; AMINO ACIDS; ANTI-BACTERIAL AGENTS; BACTERIOLYSIS; DOSE-RESPONSE RELATIONSHIP, DRUG; ERYTHROCYTES; ESCHERICHIA COLI; HEMOLYSIS; LIPOSOMES; MICROBIAL SENSITIVITY TESTS; MOLECULAR SEQUENCE DATA; PEPTIDES; PERMEABILITY; PROTEIN STRUCTURE, SECONDARY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; STEREOISOMERISM; STRUCTURE-ACTIVITY RELATIONSHIP;

BACTERIA (MICROORGANISMS); MAMMALIA;

EID: 0033555644     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00047.x     Document Type: Article

References (60)

1. Russell, P.E., Milling, R.J. & Wright, K. (1995) The need for new antibiotics: possible ways forward. In Fifty Years of Antimicrobials: Past Perspectives and Future Trends (Hunter, P.A., Darby, G.K. & Russell, N.J., ed.), pp. 67-85, Cambridge University Press.
2. Saberwal, G. & Nagaraj, R. (1994) Cell-lytic and antibacterial peptides that act by perturbing the barrier function of membranes: facets of their conformational features, structure-function correlations and membrane-perturbing abilities, Biochim. Biophys. Acta 1197, 109-131.
3. Boman, H.G. (1995) Peptide antibiotics and their role in innate immunity. Annu. Rev. Immun. 13, 61-92.
4. Nicolas, P. & Mor, A. (1995) Peptides as weapons against microorganisms in the chemical defense system of vertebrates. Annu. Rev. Microbiol. 49, 277-304.
5. Gudmundsson, G.H., Agerberth, B., Odeberg, J., Bergman, T., Olsson, B. & Salcedo, R. (1996) The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes. Eur. J. Biochem. 238, 325-332.
6. Frohm, M., Agerberth, B., Ahangari, G., Stahle-Backdahl, M., Liden, S., Wigzell, H. & Gudmundsson, G.H. (1997) The expression of the gene coding for the antibacterial peptide LL-37 is induced in human keratinocytes during inflammatory disorders. J. Biol. Chem. 272, 15258-15263.
7. Steiner, H., Hultmark, D., Engstrom, A., Bennich, H. & Boman, H.G. (1981) Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature 292, 246-248.
8. 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 U.S.A 84, 5449-5453.
9. Mor, A., Nguyen, V.H., Delfour, A., Migliore, S.D. & Nicolas, P. (1991) Isolation, amino acid sequence, and synthesis of dermaseptin, a novel antimicrobial peptide of amphibian skin. Biochemistry 30, 8824-8830.
10. Segrest, J.P., De Loof, H., Dohlman, J.G., Brouillette, C.G. & Anantharamaiah, G.M. (1990) Amphipathic helix motif: classes and properties. Proteins 8, 103-117.
11. Bessalle, R., Haas, H., Goria, A., Shalit, I. & Fridkin, M. (1992) Augmentation of the antibacterial activity of magainin by positive-charge chain extension. Antimicrob. Agents Chemother. 36, 313-317.
12. Andreu, D., Merrifield, R.B., Steiner, H. & Boman, H.G. (1985) N-terminal analogues of cecropin A: synthesis, antibacterial activity, and conformational properties. Biochemistry 24, 1683-1688.
13. Sitaram, N., Chandy, M., Pillai, V.N. & Nagaraj, R. (1992) Change of glutamic acid to lysine in a 13-residue antibacterial and hemolytic peptide results in enhanced antibacterial activity without increase in hemolytic activity. Antimicrob. Agents Chemother. 36, 2468-2472.
14. Pouny, Y., Rapaport, D., Mor, A., Nicolas, P. & Shai, Y. (1992) Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes. Biochemistry 31, 12416-12423.
15. 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.
16. Gazit, E., Boman, A., Boman, H.G. & Shai, Y. (1995) Mechanism of interaction of the mammalian antibacterial peptide cecropin PI with phospholipid vesicles. Biochemistry 34, 11479-11488.
17. Chen, H.C., Brown, J.H., Morell, J.L. & Huang, C.M. (1988) Synthetic magainin analogues with improved antimicrobial activity. FEBS Lett. 236, 462-466.
18. Blondelle, S.E. & Houghten, R.A. (1991) Hemolytic and antimicrobial activities of the twenty-four individual omission analogues of melittin. Biochemistry 30, 4671-4678.
19. Lazarovici, P., Primor, N. & Loew, L.M. (1986) Purifcation and Pore-forming activity of two hydrophobic polypeptides from the secretion of the red sea moses sole (Pardachirus marmoratus). J. Biol. Chem. 261, 16704-16713.
20. Shai, Y., Fox, J., Caratsch, C., Shih, Y.L., Edwards, C. & Lazarovici, P. (1988) Sequencing and synthesis of pardaxin, a polypeptide from the Red Sea Moses sole with ionophore activity. FEBS Lett. 242, 161-166.
21. Mor, A. & Nicolas, P. (1994) Isolation and structure of novel defensive peptides from frog skin. Eur. J. Biochem. 219, 145-154.
22. Oren, Z. & Shai, Y. (1996) Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: structure-function study. Biochemistry 36, 1826-1835.
23. Shai, Y. & Oren, Z. (1996) Diastereoisomers of cytolysins, a novel class of potent antibacterial peptides. J. Biol. Chem. 271, 7305-7308.
24. Verkleij, A.J., Zwaal, R.F., Roelofsen, B., Comfurius, P., Kastelijn, D. & Deenen, L.V. (1973) The asymmetric distribution of phospholipids in the human red cell membrane. A combined study using phospholipases and freeze-etch electron microscopy. Biochim. Biophys. Acta 323, 178-193.
25. Shaw, N. (1974) Lipid composition as a guide to the classification of bacteria. Adv. Appl. Microbiol. 17, 63-108.
26. Merrifield, R.B., Vizioli, L.D. & Boman, H.G. (1982) Synthesis of the antibacterial peptide cecropin A (1-33). Biochemistry 21, 5020-5031.
27. Shai, Y., Bach, D. & Yanovsky, A. (1990) Channel formation properties of synthetic pardaxin and analogues. J. Biol. Chem. 265, 20202-20209.
28. Sims, P.J., Waggoner, A.S., Wang, C.H. & Hoffmann, J.R. (1974) Studies on the mechanism by cyanine dyes measure membrane potential in red blood cells and phosphatidylcholine vesicles. Biochemistry 13, 3315-3330.
29. Loew, L.M., Rosenberg, I., Bridge, M. & Gitler, C. (1983) Diffusion potential cascade. Conventional detection of transferable membrane pores. Biochemistry 22, 837-844.
30. Gazit, E., Miller, I.R., Biggin, P.C., Sansom, M.S.P. & Shai, Y. (1996) Structure and orientation of the mammalian antibacterial peptide cecropin P1 within phospholipid membranes. J. Mol. Biol. 258, 860-870.
31. Harrick, N.J. (1967) Internal Reflection Spectroscopy. New York Ed, Inter-science, New York.
32. Ishiguro, R., Kimura, N. & Takahashi, S. (1993) Orientation of fusion-active synthetic peptides in phospholipid bilayers: determination by Fourier transform infrared spectroscopy. Biochemistry 32, 9792-9797.
33. Rothschild, K.J. & Clark, N.A. (1979) Anomalous amide I infrared absorption of purple membrane. Science 204, 311-312.
34. Zagorski, M.G., Norman, D.G., Barrow, C.J., Iwashita, T., Tachibana, K. & Patel, D.J. (1991) Solution structure of pardaxin P-2. Biochemistry 30, 8009-8017.
35. Li, Z.Q., Merrifield, R.B., Boman, I.A. & Boman, H.G. (1988) Effects on electrophoretic mobility and antibacterial spectrum of removal of two residues from synthetic sarcotoxin IA and addition of the same residues to cecropin B. FEBS Lett. 231, 299-302.
36. Eisenberg, D., Schwarz, E., Komaromy, M. & Wall, R. (1984) Analysis of membrane and surface protein sequences with the hydrophobic moment plot. J. Mol. Biol. 179, 125-142.
37. Pritsker, M., Jones, P., Blumenthal, R. & Shai, Y. (1998) A Synthetic All D-Amino Acid Peptide Corresponding the N-Terminal Sequence of HIV-1 gp41 Recognizes the Wild Type Fusion Peptide in the Membrane and Specifically Inhibits HIV-1 Envelope Glycoprotein-Mediated Cell Fusion. Proc. Natl. Acad. Sci. USA 95, 7287-7292.
38. Jackson, M. & Mantsch, H.H. (1995) The use and misuse of FTIR spectroscopy in the determination of protein structure. Crit. Rev. Biochem. Mol. Biol. 30, 95-120.
39. Fink, J., Merrifield, R.B., Boman, A. & Boman, H.G. (1989) The chemical synthesis of cecropin D and an analog with enhanced anti-bacterial activity. J. Biol. Chem. 264, 6260-6267.
40. Fringeli, U.P. & Gunthard, H.H. (1981) Infrared Membrane Spectroscopy (Grell, E., ed.), pp. 270-332. Springer-Verlag, Berlin.
41. Yang, P.W., Stewart, L.C. & Mantsch, H.H. (1987) Polarized attenuated total reflectance spectra of oriented purple membranes, Biochem. Biophys. Res. Commun. 145, 298-302.
42. Cameron, D.G., Casal, H.L., Gudgin, E.F. & Mantsch, H.H. (1980) The gel phase of dipalmitoyl phosphatidylcholine. An infrared characterization of the acyl chain packing. Biochim. Biophys. Acta 596, 463-467.
43. Krause, E., Beyermann, M., Dathe, M., Rothemund, S. & Bienert, M. (1995) Location of an amphipathic alpha-helix in peptides using reversed-phase HPLC retention behavior of D-amino acid analogs. Anal. Chem. 67, 252-258.
44. Rothemund, S., Beyermann, M., Krause, E., Krause, G., Bienert, M., Hodges, R.S., Sykes, B.D. & Sonnichsen, F.D. (1995) Structure effects of double D-amino acid replacements: a nuclear magnetic resonance and circular dichroism study using amphipathic model helices. Biochemistry 34, 12954-12962.
45. Lehrer, R.I., Lichtenstein, A.K. & Ganz, T. (1993) Defensins-antimicrobial and cytotoxic peptides of mammalian cells. Annu. Rev. Immun. 11, 105-128.
46. Selsted, E.M., Tang, Y.Q., Morris, W.L., McGuire, P.A., Novotny, M.J., Smith, W., Henschen, A.H. & Cullor, J.S. (1993) Purification, primary structure and, and antbacterial activites of beta-defensins, a new family of antimicrobial peptides from bovine neutrophils. J. Biol. Chem. 268, 6641-6648.
47. Hoffmann, J.A. & Hetru, C. (1992) Insect defensins: inducible antibacterial peptides. Immunol. Today 13, 411-415.
48. Kokryakov, V.N., Harwig, S.S., Panyutich, E.A, Shevchenko, A.A., Aleshina, G.M., Shamova, O.V., Korneva, H.A. & Lehrer, R.I. (1993) Protegrins: leukocyte antimicrobial peptides that combine features of corticostatic defensins and tachyplesins. FEBS Lett. 327, 231236.
49. Nakamura, T., Furunaka, H., Miyata, T., Tokunaga, F., Muta, T., Iwanaga, S., Niwa, M., Takao, T. & Shimonishi, Y. (1988) Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus). Isolation and chemical structure. J. Biol. Chem. 263, 16709-16713.
50. Andersson, M., Gunne, H., Agerberth, B., Boman, A., Bergman, T., Sillard, R., Jornvall, H., Mutt, V., Olsson, B., Wigzell, H.lysin, a novel effector peptide of cytotoxic T and NK cells. Structure and cDNA cloning of the porcine form, induction by interleukin 2, antibacterial and antitumour activity. EMBO J. 14, 1615-1625.
51. Tamamura, H., Ikoma, R., Niwa, M., Funakoshi, S., Murakami, T. & Fujii, N. (1993) Antimicrobial activity and conformation of tachyplesin I and its analogs. Chem. Pharm. Bull (Tokyo) 41, 978-980.
52. Qu, X.D., Harwig, S.S.L., Shafer, W.M. & Lehrer, R.I. (1997) Protegrin structure and activity against Neisseria gonorrhoeae. Infect. Immun. 65, 636-639.
53. Andersson, M., Holmgren, A. & Spyrou, G. (1996) NK-lysin, a disulfide-containing effector peptide of T-lymphocytes, is reduced and inactivated by human thioredoxin reductase. Implication for a protective mechanism against NK-lysin cytotoxicity. J. Biol. Chem. 271, 10116-10120.
54. Matsuzaki, K., Harada, M., Funakoshi, S., Fujii, N. & Miyajima, K. (1991) Physicochemical determinants for the interactions of magainins 1 and 2 with acidic lipid bilayers. Biochim. Biophys. Acta 1063, 162-170.
55. Wieprecht, T., Dathe, M., Schumann, M., Krause, E., Beyermann, M. & Bienert, M. (1996) Conformational and functional study of magainin 2 in model membrane environments using the new approach of systematic double-D-amino acid replacement. Biochemistry 35, 10844-10853.
56. Oren, Z. & Shai, Y. (1996) A class of highly potent antibacterial peptides derived from pardaxin, a pore-forming peptide isolated from Moses sole fish Pardachirus marmoratus. Eur. J. Biochem. 237, 303-310.
57. Kiyota, T., Lee, S. & Sugihara, G. (1996) Design and synthesis of amphiphilic α-helical model peptides with systematically varied hydrophobic-hydrophilic balance and their interaction with lipid and bio-membranes. Biochemistry 35, 13196-13204.
58. Castano, S., Desbat, B., Cornut, I., Meleard, P. & Dufourcq, J. (1997) α-helix to β-sheet transition within the LeuiLysj (i=2j) series of lytic amphipathic peptides by decreasing their size. Lett. Pep. Sci. 195-200.
59. Epand, R.M. (1993) The Amphipathic Helix, pp, 15-165. CRC Press, Boca Raton, FL.
60. Shai, Y. (1995) Molecular recognition between membrane-spanning helices. Trends Bio. Sci. 20, 460-464.