Consequences of introducing a disulfide bond into an antibacterial and hemolytic peptide

Journal of Peptide Research

Volumn 54, Issue 6, 1999, Pages 528-535

  Krishnakumari, V ^a   Sharadadevi, A ^a   Sitaram, N ^a   Nagaraj, R ^a  

^a CENTRE FOR CELLULAR AND MOLECULAR BIOLOGY   (India)

Author keywords

Antibacterial peptides; Distorted helix; Disulfide bond; Hemolytic activity; Membrane binding

Indexed keywords

POLYPEPTIDE ANTIBIOTIC AGENT;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; DISULFIDE BOND; ERYTHROCYTE MEMBRANE; HEMOLYSIS; MEMBRANE BINDING; NONHUMAN; PEPTIDE ANALYSIS; PRIORITY JOURNAL; RAT;

AMINO ACID SEQUENCE; ANTI-BACTERIAL AGENTS; CIRCULAR DICHROISM; DISULFIDES; HEMOLYSIS; MEMBRANES, ARTIFICIAL; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN CONFORMATION;

EID: 0032753413     PISSN: 1397002X     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1399-3011.1999.00133.x     Document Type: Article

References (52)

1. Lehrer, R.I., Lichtenstein, A.K. & Ganz, T. (1993) Defensins: antimicrobial and cytotoxic peptides of mammalian cells. Annu. Rev. Immunol. 11, 105-128.
2. Boman, H. (1995) Peptide antibiotics and their role in innate immunity. Annu. Rev. Immunol. 13, 61-92.
3. Nicolas, P. & Mor, A. (1995) Peptides as weapons against microorganisms in the chemical defense system of vertebrates. Annu. Rev. Immunol. 49, 277-304.
4. Maloy, W.L. & Kari, U.P. (1995) Structure-activity studies on magainins and other host defense peptides. Biopolymers 37, 105-122.
5. Saberwal, G. & Nagaraj, R. (1994) Cell lyric 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, 109-132.
6. Hancock, R.E.W. (1997) Peptide antibiotics. Lancet 349, 418-422.
7. Holak, T.A., Engstrom, 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.
8. Marion, D., Zasloff, M. & Bax, A. (1988) A two dimensional NMR study of the antimicrobial peptide magainin 2. FEBS Lett. 227, 21-26.
9. White, S.H., Wimley, W.C. & Selsted, M.E. (1995) Structure, function and membrane integration of defensins. Curr. Opin. Struct. Biol. 5, 521-527.
10. Kawano, K., Yonega, T., Miyata, T., Yoshikawa, K., Tokunaga, F., Tenada, Y. & Iwanaga, S. (1990) Antimicrobial peptide tachyplesin I isolated from hemolytes of the horseshoe crab (Tachypleus tridentatus) NMR determination of the beta-sheet structure. J. Biol. Chem. 265, 15365-15367.
11. Harwig, S.S.L., Swiderek, K.M., Lee, T.D. & Lehrer, R.I. (1995) Determination of disulphide bridges in PG-2 an antimicrobial peptide from porcine leukocytes. J. Peptide Sci. 3, 207-215.
12. Harwig, S.S.L., Waring, A., Yang, H.J., Cho, Y., Tan, L. & Lehrer, R.I. (1998) Intramolecular disulphide bonds enhance the antibacterial and lytic activities of protegrins at physiological sodium chloride concentration. Eur. J. Biochem. 240, 352-357.
13. 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, 1683-1687.
14. 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.
15. 2 terminal α-helical domain 1-18 of dermaseptin is responsible for antimicrobial activity. J. Biol. Chem. 269, 1934-1939.
16. Bessale, R., Kapitkovsky, A., Shalit, I. & Fridkin, M. (1990) All D-magainin: Chirality, antimicrobial activity and proteolytic resistance. FEBS Lett. 274, 151-155.
17. Wade, D., Boman, A., Wahlin, B., Drain, C.M., Andreu, D., Boman, H.G. & Merrifield, R.B. (1990) All D-amino acid containing channel-forming antibiotic peptides. Proc. Natl. Acad. Sci. USA 87, 4761-4765.
18. Merrifield, R.B., Juvvadi, P., Andreu, D., Ubach, J., Boman, A. & Boman, H.G. (1995). Retro and retroenantio analogs of cecropin-melittin hybrids. Proc. Natl. Acad. Sci. USA 92, 3449-3453.
19. Shai, Y. & Oren, Z. (1996) Diaseteromers of cytolysins, a novel class of potent antibacterial peptides. J. Biol. Chem. 271, 7305-7308.
20. Juvvadi, P., Vunnam, S. & Merrifleld, R.B. (1996) Synthetic melittin its enantio, retro and retero enantio isomers and selected chimeric analog: their antibacterial, hemolytic and lipid bilayer interaction. J. Am. Chem. Soc. 118, 8989-8997.
21. Andreu, D., Ubach, J., Boman, A., Wahlin, B., Wade, O., Merrifield, R.B. & Boman, H.G. (1992) Shortened cecropin A melittin hybrids. Significant size reduction retains potent antibiotic activity. FEBS Lett. 296, 190-194.
22. Wade, D., Andreu, D., Mitchell, S.A., Silveria, A.M.V., Boman, A., Boman, H.G. & Merrifield, R.B. (1992) Antibacterial peptides designed as analogs or hybrids of ceeropins and mellitin. Int. J. Peptide Protein Res. 40, 429-436.
23. Blondelle, S.E., Perez-Paya, E. & Houghten, R.A. (1996) Synthetic combinatorial libraries: novel discovery strategy for identification of antimicrobial agents. Antimic. Agents Chemother. 40, 1067-1071.
24. Matsuzaki, K., Yoneyama, S., Fuju, N., Miyajima, K., Yamada, K., Ikirino, Y. & Anzai, K. (1997) Membrane permeabilization mechanisms of a cyclic antimicrobial peptide. Biochemistry 36, 9799-9806.
25. Sitaram, N., Chandy, M., Pillai, V.N.R. & 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. Antimic. Agents Chemother. 36, 2468-2472.
26. Sitaram, N. & Nagaraj, R. (1990) A synthetic 13-residue peptide corresponding to the hydrophobic region of bovine seminalplasmin has antibacterial activity and also causes lysis of red blood cells. J. Biol. Chem. 265, 10438-10442.
27. Reddy, E.S.P. & Bhargava, P.M. (1979) Seminalplasmin an antimicrobial protein from bovine seminal plasma which acts in E. coli by specific inhibition of RNA synthesis. Nature 279, 725-728.
28. Sitaram, N., Krishnakumari, V. & Bhargava, P.M. (1986) Seminalplasmin and caltrin are the same protein. FEBS Lett. 20, 233-236.
29. Atherton, E. & Sheppard, R.C. (1989) Solid Phase Peptide Synthesis: A Practical Approach. IRL, Oxford.
30. Veher, D.F., Milkowski, J.D., Vargas, S.L., Denkelwalter, R.G. & Hirshmann (1972). Acetamidomethyl: a novel thiol protecting group for cysteine. J. Am. Chem. Soc. 94, 5456-5461.
31. Tam, J.P., Wu, C. R., Liu, W. & Zhang, J.W. (1991) Disulfide bond formation in peptides by dimethyl sulfoxide scope and application. J. Am. Chem. Soc. 113, 6657-6662.
32. Sims, P.J., Waggoner, A.S., Wang, C.-H. & Hoffman, J.C. (1974) Studies on the mechanism by which cyanine dyes measure membrane potential in red blood cells and phosphatidylcholine vesicles. Biochemistry 13, 3315-3329.
33. Rizzo, V.C.S., Stanowsky and G. & Schwarz (1987) Alamethicin incorporation in lipid bilayer: a thermodynamic study. Biochemistry 26, 2751-2759.
34. Beschiaschvili, G. & Sceelig, J. (1990) Melittin binding to mixed phosphatidylglycerol/phosphatidylcholine membranes. Biochemistry 29, 52-58.
35. Rapoport, D. & Shai, Y. (1991) Interaction of fluorescently labelled pardaxin and its analogues with lipid bilayers. J. Biol. Chem. 266, 23769-23775.
36. Perezel, A. & Hollossi, M. (1996) In Circular Dichroism and the Conformational Analysis of Biomolecules (Fasman, G.D., ed.). Plenum Press, New York, pp. 261-281.
37. Yang, J.J., Buck, M., Pitkcathly, M., Kotik, M., Haynie, D.T., Dobson, C.M. & Redford, S.E. (1995) The conformational properties of four peptides spanning the sequence of hen lysozyme. J. Mol. Biol. 252, 483-491.
38. Manning, M.C., Illangasekare, M. & Woody, R.W. (1988) Circular dichroism studies of distorted α-helices, twisted β-sheets and γ-turn. Biophys. Chem. 31, 77-86.
39. Morris, A.L., MacArthur, M.W., Hutchinson, E.G. & Thornton, J.M. (1992) Stereochemical quality of protein structure coordinates. Proteins: Struct. Funct. Genet. 12, 345-364.
40. Sowdhamini, R., Ramakrishnan, C. & Balaram, P. (1993) Modelling multiple disulphide loop containing polypeptides by random conformation generation the test cases for α-conotoxin G1 and endothelin 1. Protein Eng. 6, 873-882.
41. Gunasekaran, K., Ramakrishnan, C. & Balaram, P. (1996) Disallowed Ramachandran conformation of amino acid residues in protein structures. J. Mol. Biol. 264, 191-198.
42. 2+ and the interaction of pore formers with membranes. J. Biosci. 8, 273-292.
43. Simmaco, M., Mignogua, G., Barra, D. & Bossa, F. (1994) Antimicrobial peptides from skin secretions of Rana esculenta. J. Biol. Chem, 269, 11956-11961.
44. Fehlbaum, P., Bulet, P., Chemysh, S., Briand, J.-P., Roussel, J.P., Letelbier, L., Hetru, C. & Hoffmann, J.A. (1996) Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides. Proc. Natl. Acad. Sci. USA 93, 1221-1225.
45. Mangoni, M.E., Aumelas, A., Charnet, P., Roumestand, C., Cluchi, L., Despaux, E., Brassy, G., Calas, B. & Chavanier, A. (1996) Change in membrane permeability induced by protegrin 1: implication of disulphide bridges for pore formation. FEBS Lett. 383, 93-98.
46. Rietman, B.H., Folkers, P.J.M., Folmer, R.H.A., Tesser, G.I. & Hilbeu, C.W. (1996) The solution structure of synthetic circular peptide CGVSRQGKPYC. Eur. J. Chew. 238, 706-713.
47. Gunasekaran, K., Ramakrishnan, C. & Balaram, P. (1997) Beta hairpins in proteins revisited: lessons for de novo design. Protein Eng. 10, 1131-1141.
48. Blanco, F., Ramirez-Alvendo, M. & Serrano, L. (1998) Formation and stability of beta hairpin structures in polypeptides. Curt. Opin. Struct. Biol. 8, 107-111.
49. Hutchinson, E.G. & Thornton, J.M. (1994) A revised set of potentials for beta turn formation in protein. Protein Sci. 3, 2207-2216.
50. Guddat, L.W., Martin, J.A., Shan, L., Edmundson, A.B. & Gray, W.R. (1996) Three dimensional structure of alpha conotoxin at 1.2A resolution. Biochemistry 35, 11329-11335.
51. Oren, Z. & Shai, Y. (1997) Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: structure function study. Biochemistry 36, 1826-1835.
52. Thennarasu, S. & Nagaraj, R. (1995) Design of 16-residue peptides possessing antimicrobial and hemolytic activities or only antimicrobial activity from an inactive peptide. Int. J. Peptide Protein. Res. 46, 480-486.