Indolicidin-derived antimicrobial peptide analogs with greater bacterial selectivity and requirements for antibacterial and hemolytic activities

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1794, Issue 2, 2009, Pages 185-192

  Kim, Sung Min ^a   Kim, Joung Min ^a   Joshi, Bishnu Prasad ^a   Cho, Hyeongjin ^a   Lee, Keun Hyeung ^a  

^a Inha University   (South Korea)

Author keywords

Antibacterial peptide; Antimicrobial activity; Indolicidin; Reduced amide bond; Secondary structure; Selectivity; Stability

Indexed keywords

INDOLICIDIN; POLYPEPTIDE ANTIBIOTIC AGENT; TRYPSIN;

ANTIBACTERIAL ACTIVITY; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; CYTOLYSIS; DRUG DESIGN; DRUG SYNTHESIS; ERYTHROCYTE; HUMAN; HUMAN CELL; HYDROGEN BOND; PRIORITY JOURNAL; PROTEIN STABILITY; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; ANTI-BACTERIAL AGENTS; ANTIFUNGAL AGENTS; ANTIMICROBIAL CATIONIC PEPTIDES; CIRCULAR DICHROISM; DRUG DESIGN; HEMOLYSIS; HUMANS; HYDROGEN BONDING; MICROBIAL SENSITIVITY TESTS; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; STRUCTURE-ACTIVITY RELATIONSHIP;

BACTERIA (MICROORGANISMS);

EID: 58149178538     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.10.009     Document Type: Article

References (44)

1. Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 415 (2002) 389-395
2. Selsted M.E., Novotny M.J., Morris W.L., Tang Y., Smith W., and Cullor J.S. Indolicidin, a novel bactericidal tridecapeptide amide from neutrophils. J. Biol. Chem. 267 (1992) 4292-4295
3. Lee D.G., Kim H.K., Kim S.A., Park Y., Park S.C., Jang S.H., and Hahm K.S. Fungicidal effect of indolicidin and its interaction with phospholipid membranes. Biochem. Biophys. Res. Commun. 305 (2003) 305-310
4. Aley S.B., Zimmerman M., Hetsko M., Selsted M.E., and Gillin F.D. Killing of giardia lamblia by cryptdins and cationic neutrophil peptides. Infect. Immun. 62 (1994) 5397-5403
5. Robinson Jr W.E., McDougall B., Tran D., and Selsted M.E. Anti-HIV-1 activity of indolicidin, an antimicrobial peptide from neutrophils. J. Leukocyte Biol. 63 (1998) 94-100
6. Schluesener H.J., Radermacher S., Melms A., and Jung S. Leukocytic antimicrobial peptides kill autoimmune T cells. J. Neuroimmunol. 47 (1993) 199-202
7. Chan D.I., Prenner E.J., and Vogel H.J. Tryptophan- and arginine-rich antimicrobial peptides: Structures and mechanisms of action. Biochim. Biophys. Acta. 1758 (2006) 1184-1202
8. Marchand C., Krajewski K., Lee H., Antony S., Johnson A.A., Amin R., Roller P., Kvaratskhelia M., and Pommier Y. Covalent binding of the natural antimicrobial peptide indolicidin to DNA abasic sites. Nucleic Acids Res. 34 (2006) 5157-5165
9. Hsu C., Chen C., Jou M., Lee A.Y., Lin Y., Yu Y., Huang W., and Wu S. Structural and DNA-binding studies on the bovine antimicrobial peptide, indolicidin: evidence for multiple conformations involved in binding to membranes and DNA. Nucleic Acids Res. 33 (2005) 4053-4064
10. Ladokhin A.S., Selsted M.E., and White S.H. CD spectra of indolicidin antimicrobial peptides suggest turns, not polyproline helix. Biochemistry 38 (1999) 12313-12319
11. Andrushchenko V.V., Vogel H.J., and Prenner E.J. Solvent-dependent structure of two tryptophan-rich antimicrobial peptides and their analogs studied by FTIR and CD spectroscopy. Biochim. Biophys. Acta. 1758 (2006) 1596-1608
12. Falla T.J., Karunaratne D.N., and Hancock R.E.W. Mode of action of the antimicrobial peptide indolicidin. J. Biol. Chem. 271 (1996) 19298-19303
13. Ryge T.S., Doisy X., Ifrah D., Olsen J.E., and Hansen P.R. New indolicidin analogues with potent antibacterial activity. J. Pept. Res. 64 (2004) 171-185
14. Staubitz P., Peschel A., Nieuwenhuizen W.F., Otto M., Götz F., Jung G., and Jack R.W. Structure-function relationships in the tryptophan-rich, antimicrobial peptide indolicidin. J. Pept. Sci. 7 (2001) 552-564
15. Subbalakshmi C., Bikshapathy E., Sitaram N., and Nagaraj R. Antibacterial and hemolytic activities of single tryptophan analogs of indolicidin. Biochem. Biophys. Res. Commun. 274 (2000) 714-716
16. Friedrich C.L., Rozek A., Patrzykat A., and Hancock R.E.W. Structure and mechanism of action of an indolicidin peptide derivative with improved activity against gram-positive bacteria. J. Biol. Chem. 276 (2001) 24015-24022
17. Ösapay K., Tran D., Ladokhin A.S., White S.H., Henschen A.H., and Selsted M.E. Formation and characterization of a single Trp-Trp cross-link in indolicidin that confers protease stability without altering antimicrobial activity. J. Biol. Chem. 275 (2000) 12017-12022
18. Rozek A., Powers J.P., Friedrich C.L., and Hancock R.E.W. Structure-based design of an indolicidin peptide analogue with increased protease stability. Biochemistry 42 (2003) 14130-14138
19. Fields G.B., and Noble R.L. Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids. Int. J. Pept. Protein Res. 35 (1990) 161-214
20. Park M.S., Oh H.S., Cho H.J., and Lee K.H. Microwave-assisted solid-phase synthesis of pseudopeptides containing reduced amide bond. Tetrahedron Lett. 48 (2007) 1053-1057
21. Mayer L.D., Hope M.J., and Cullis P.R. Vesicles of variable sizes produced by a rapid extrusion procedure. Biochim. Biophys. Acta 858 (1986) 161-168
22. Harwick H.J., Kalmanson G.M., and Guze L.B. In vitro activity of ampicillin or vancomycin combined with gentamicin or streptomycin against enterococci. Antimicrob. Agents Chemother. 4 (1973) 383-387
23. Cheron M., Cybulska B., Mazerski J., Grzybowska J., Czerwinski A., and Borowski E. Quantitative structure-activity relationships in amphotericin B derivatives. Biochem. Pharmacol. 37 (1988) 827-836
24. Frecer V. QSAR Analysis of antimicrobial and haemolytic effects of cyclic cationic antimicrobial peptides derived from protegrin-1. Bioorg. Med. Chem. 14 (2006) 6065-6074
25. Dathe M., Wieprecht T., Nikolenko H., Handel L., Maloy W.L., Macdonald D.L., Beyermann M., and Bienert M. Hydrophobicity, hydrophobic moment and angle subtended by charged Residues modulate antibacterial and haemolytic activity of amphipathic helical peptides. FEBS Lett. 403 (1997) 208-212
26. Kwon M.Y., Hong S.Y., and Lee K.H. Structure-activity analysis of brevinin 1E amide, an antimicrobial peptide from Rana esculenta. Biochim. Biophys. Acta 1387 (1998) 239-248
27. Oren Z., Jiang H., and Shai Y. A repertoire of novel antibacterial diastereomeric peptides with selective cytolytic activity. J. Biol. Chem. 272 (1997) 14643-14649
28. Vanderesse R., Grand V., Limal D., Vicherat A., Marraude M., Didierjean C., and Aubry A. Structural comparison of homologous reduced peptide, reduced azapeptide, iminoazapeptide, and methyleneoxypeptide analogues. J. Am. Chem. Soc. 120 (1998) 9444-9451
29. Oh J., and Lee K.H. Characterization of the unique function of a reduced amide cytolytic peptide that acts on phospholipid membranes. Biochem. J. 352 (2000) 659-666
30. Krause E., Beyermann M., Dathe M., Rothemund S., and Bienert M. Location of an amphipathic alpha-helix in peptides using reversed-phase HPLC retention behavior of d-amino acid analogs. Anal. Chem. 67 (1995) 252-258
31. Wu C.C., Ikeda K., and Yang J.T. Ordered conformation of polypeptides and proteins in acidic dodecyl sulfate solution. Biochemistry 20 (1981) 566-570
32. Berova N., Nakanishi K., and Woody R.W. Circular Dichroism Chapter 21 (2000), Wiley-VCH, New York 601-620
33. Grishina I.B., and Woody R.W. Contributions of tryptophan side chains to the circular dichroism of globular proteins: exciton couplets and coupled oscillators. Faraday Discuss 99 (1994) 245-262
34. Rozek A., Fredrich C.L., and Hancock R.E.W. Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles. Biochemistry 39 (2000) 15744-15765
35. Hristova K., Selsted M.E., and White S.H. Critical role of lipid composition in membrane permeabilization by rabbit neutrophil defensins. J. Biol. Chem. 272 (1997) 24224-24233
36. Guidotti G. Membrane proteins. Annu. Rev. Biochem. 41 (1972) 731-752
37. Vogel H. Incorporation of melittin into phosphatidylcholine bilayers. Study of binding and conformational changes. FEBS Lett. 134 (1981) 37-42
38. Kiyota T., Lee S., and Sugihara G. Design and synthesis of amphiphilic alpha-helical model peptides with systematically varied hydrophobic-hydrophilic balance and their interaction with lipid- and bio-membranes. Biochemistry 35 (1996) 13196-13204
39. Oren Z., and Shai Y. Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: structure-function study. Biochemistry 36 (1997) 1826-1835
40. Matsuzaki K. Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes. Biochim. Biophys. Acta 1462 (1999) 1-10
41. Shai Y. From innate immunity to de-novo designed antimicrobial peptides. Curr. Pharm. Design 8 (2002) 715-725
42. Bruehlmeier M., Garcia-Garayoa E., Blanc A., Holzer B., Gergely S., Tourwe D., Schubiger P.A., and Blauenstein P. Stabilization neurotensin analogues: effect on peptide catabolism, biodistribution and tumor binding. Nucl. Med. Biol. 29 (2002) 321-327
43. Oh J., Hong S.Y., and Lee K.H. A Comparison of characteristics between membrane-active antifungal peptide and its pseudopeptides. Bioorg. Med. Chem. 11 (1999) 2509-2515
44. Chen Y.C., Muhlrad A., Shteyer A., Vidson M., Bab I., and Chorev M. Bioactive pseudopeptidic analogues and cyclostereoisomers of osteogenic growth peptide c-terminal pentapeptide, OGP(10-14) J. Med. Chem. 44 (2002) 1624-1632