Structure-function analyses involving palindromic analogs of tritrypticin suggest autonomy of anti-endotoxin and antibacterial activities

Protein Science

Volumn 17, Issue 3, 2008, Pages 545-554

  Kaur, Kanwal J ^a   Sarkar, Pampi ^a   Nagpal, Sushma ^a   Khan, Tarique ^a   Salunke, Dinakar M ^a  

^a NATIONAL INSTITUTE OF IMMUNOLOGY   (India)

Author keywords

Antibacterial peptides; Bacterial infection; Endotoxin shock; Structure function studies; Synthesis of peptides and proteins

Indexed keywords

ANTIINFECTIVE AGENT; ARGINYLARGINYLPHENYLALANYLPROLYLTRYPTOPHYLTRYPTOPHYLTRYPTOPHAN; CATHELICIDIN; ENDOTOXIN ANTIBODY; LIPOPOLYSACCHARIDE; TRITRYPTICIN DERIVATIVE; TRYPTOPHYLTRYPTOPHYLTRYPTOPHYLPROLYLPHENYLALANYLARGINYLARGININE; UNCLASSIFIED DRUG;

ANTIBACTERIAL ACTIVITY; ARTICLE; DRUG PROTEIN BINDING; DRUG STRUCTURE; HYDROPHOBICITY; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION;

ANTI-BACTERIAL AGENTS; B-LYMPHOCYTES; CELL PROLIFERATION; LIPOPOLYSACCHARIDES; NITRIC OXIDE; OLIGOPEPTIDES; PEPTIDES; POLYMYXIN B; STRUCTURE-ACTIVITY RELATIONSHIP;

BACTERIA (MICROORGANISMS);

EID: 39549086322     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.073145008     Document Type: Article

References (27)

1. Boman, H.G., Agerberth, B., and Boman, A. 1993. Mechanism of action on Escherichia coli of Cecropin P1 and PR-39, two antibacterial peptides from pig intestine. Infect. Immun. 61: 2978-2984.
2. Casteels, P. and Tempst, P. 1994. Apidaecin-type peptide antibiotics function through a non-poreforming mechanism involving stereospecificity. Biochem. Biophys. Res. Commun. 199: 339-345.
3. de Haas, C.J., Haas, P.J., van Kessel, K.P., and van Strijp, J.A. 1998. Affinities of different proteins and peptides for lipopolysaccharide as determined by biosensor technology. Biochem. Biophys. Res. Commun. 252: 492-496.
4. Falla, T.J., Karunaratne, D.N., and Hancock, R.E.W. 1996. Mode of action of the antimicrobial peptide Indolicidin. J. Biol. Chem. 271: 19298-19303.
5. Gallo, R.L., Ono, M., Povsic, T., Page, C., Eriksson, E., Klagsbrun, M., and Bernfield, M. 1994. Syndecans, cell surface heparan sulfate proteoglycans, are induced by a proline-rich antimicrobial peptide from wounds. Proc. Natl. Acad. Sci. 91: 11035-11039.
6. Gao, Y., Lecker, S., Post, M.J., Hietaranta, A.J., Li, J., Volk, R., Li, M., Sato, K., Saluja, A.K., Steer, M.L., et al. 2000. Inhibition of ubiquitin-proteasome pathway-mediated IκBα degradation by a naturally occurring antibacterial peptide. J. Clin. Invest. 106: 439-448.
7. Gudmundsson, G.H. and Agerberth, B. 1999. Neutrophil antibacterial peptides, multifunctional effector molecules in the mammalian immune system. J. Immunol. Methods 232: 45-54.
8. Hancock, R.E.W. 1997. Peptide antibiotics. Lancet 349: 418-422.
9. Hancock, R.E.W. and Scott, M.G. 2000. The role of antimicrobial peptides in animal defenses. Proc. Natl. Acad. Sci. 97: 8856-8861.
10. Hancock, R.E.W., Falla, T., and Brown, M.M. 1995. Cationic bactericidal peptides. Adv. Microb. Physiol. 37: 135-175.
11. Kirikae, T., Hirata, M., Yamasu, H., Kirikae, F., Tamura, H., Kayama, F., Nakatsuka, K., Yokochi, T., and Nakano, M. 1998. Protective effects of a human 18-kilodalton cationic antimicrobial protein (CAP18)- derived peptide against murine endotoxemia. Infect. Immun. 66: 1861-1868.
12. Ludkte, S.J., He, K., Heller, W.T., Harroun, T.A., Yang, L., and Huang, H.W. 1996. Membrane pores induced by Magainin. Biochemistry 35: 13723-13728.
13. Medzhitov, R. and Janeway Jr., C. 2000. Innate immunity. N. Engl. J. Med. 3: 338-344.
14. Moore, R.A., Bates, N.C., and Hancock, R.E.W. 1986. Interaction of polycationic antibiotics with Pseudomonas aeruginosa lipopolysaccharide and lipid A studied by using dansyl-polymyxin. Antimicrob. Agents Chemother. 29: 496-500.
15. Nagpal, S., Gupta, V., Kaur, K.J., and Salunke, D.M. 1999. Structure-function analysis of tritrypticin, an antibacterial peptide of innate immune origin. J. Biol. Chem. 274: 23296-23304.
16. Nagpal, S., Kaur, K.J., Jain, D., and Salunke, D.M. 2002. Plasticity in structure and interactions is critical for the action of indolicidin, an antibacterial peptide of innate immune origin. Protein Sci. 11: 2158-2167.
17. Okuda, D., Yomogida, S., Tamura, H., and Nagaoka, I. 2006. Determination of the antibacterial and lipopolysaccharide-neutralizing regions of guinea pig neutrophil cathelicidin peptide CAP11. Antimicrob. Agents Chemother. 50: 2602-2607.
18. Piers, K.L., Brown, M.H., and Hancock, R.E.W. 1994. Improvement of outer membrane-permeabilization and lipopolysaccharide-binding activities of an antimicrobial cationic peptide by C-terminal modification. Antimicrob. Agents Chemother. 38: 2311-2316.
19. Rosenfeld, Y., Papo, N., and Shai, Y. 2006. Endotoxin (LPS) neutralization by innate immunity host-defense peptides: Peptides' properties and plausible modes of action. J. Biol. Chem. 281: 1636-1643.
20. Schibli, D.J., Hwang, P.M., and Vogel, H.J. 1999. Structure of the antimicrobial peptide tritrpticin bound to micelles: A distinct membrane-bound peptide fold. Biochemistry 38: 16749-16755.
21. Schindler, P.R.G. and Teuber, M. 1975. Action of polymyxin B on bacterial membranes: Morphological changes in the cytoplasm and in the outer membrane of Salmonella typhimurium and Escherichia coli B. Antimicrob. Agents Chemother. 8: 94-104.
22. Shai, Y. 1995. Molecular recognition between membrane-spanning polypeptides. Trends Biochem. Sci. 20: 460-464.
23. Skerlavaj, B., Romeo, D., and Gennaro, R. 1990. Rapid membrane permeabilization and inhibition of vital functions of Gram-negative bacteria by Bactenecins. Infect. Immun. 58: 3724-3730.
24. Woody, R.W. 1985. Circular dichroism of peptides. In The peptides: Analysis, synthesis, biology (eds. S. Udenfriend et al.), Vol. 7, pp. 15-114. Academic Press, London.
25. Yang, S.T., Jeon, J.H., Kim, Y., Shin, S.Y., Hahm, K.S., and Kim II, J. 2006. Possible role of a PXXP central hinge in the antibacterial activity and membrane interaction of PMAP-23, a member of cathelicidin family. Biochemistry 45: 1775-1784.
26. Zarember, K.A., Katz, S.S., Tack, B.F., Doukhan, L., Weiss, J., and Elsbach, P. 2002. Host defense functions of proteolytically processed and parent (unprocessed) cathelicidins of rabbit granulocytes. Infect. Immun. 70: 569-576.
27. Zasloff, M. 2002. Antimicrobial peptides of multicellular organisms. Nature 415: 389-395.