Selective membrane disruption: Mode of action of C16G2, a specifically targeted antimicrobial peptide

Antimicrobial Agents and Chemotherapy

Volumn 55, Issue 7, 2011, Pages 3446-3452

  Kaplan, Christopher W ^a   Sim, Jee Hyun ^a   Shah, Kevin R ^a   Kolesnikova Kaplan, Aida ^b   Shi, Wenyuan ^b   Eckert, Randal ^a  

^a C3 Jian Inc   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; C16G2; CARIOGENIC AGENT; MELITTIN; MELITTIN B; NOVISPIRIN G10; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

ANTIMICROBIAL ACTIVITY; ARTICLE; BACTERIAL MEMBRANE; BACTERICIDAL ACTIVITY; CELL DEATH; CELL DISRUPTION; CELL KILLING; CELL MEMBRANE POTENTIAL; CONTROLLED STUDY; CYTOTOXICITY; DRUG DESIGN; DRUG MECHANISM; DRUG SELECTIVITY; DRUG SPECIFICITY; MEMBRANE DAMAGE; MIXED CELL CULTURE; NONHUMAN; PRIORITY JOURNAL; STREPTOCOCCUS MUTANS;

ANTI-BACTERIAL AGENTS; ANTI-INFECTIVE AGENTS; ANTIMICROBIAL CATIONIC PEPTIDES; MELITTEN; MICROBIAL SENSITIVITY TESTS; STREPTOCOCCUS; STREPTOCOCCUS MUTANS;

EID: 79959213007     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.00342-11     Document Type: Article

References (41)

1. Anderson, M. H., and W. Shi. 2006. A probiotic approach to caries management. Pediatr. Dent. 28:151-153, 192-198.
2. Anonymous. 2008. National health expenditure projections 2008-2018. Centers for Medicare and Medicaid Services, Office of the Actuary, Baltimore, MD.
3. Bechinger, B. 1997. Structure and functions of channel-forming peptides: magainins, cecropins, melittin and alamethicin. J. Membr. Biol. 156:197-211.
4. Bechinger, B. 1999. The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy. Biochim. Biophys. Acta 1462:157-183.
5. Beighton, D. 2005. The complex oral microflora of high-risk individuals and groups and its role in the caries process. Community Dent. Oral Epidemiol. 33:248-255.
6. Corby, P. M., et al. 2005. Microbial risk indicators of early childhood caries. J. Clin. Microbiol. 43:5753-5759.
7. Cowell, N. D., A. R. Allen, and B. Jarvis. 1971. The in vivo effect of nisin on the microflora of the oral cavity. J. Appl. Bacteriol. 34:787-791.
8. Eckert, R., et al. 2006. Targeted killing of Streptococcus mutans by a pheromone-guided "smart" antimicrobial peptide. Antimicrob. Agents Chemother. 50:3651-3657.
9. Eckert, R., et al. 2006. Adding selectivity to antimicrobial peptides: rational design of a multidomain peptide against Pseudomonas spp. Antimicrob. Agents Chemother. 50:1480-1488.
10. Evans, C. A., and D. V. Kleinman. 2000. The Surgeon General's report on America's oral health: opportunities for the dental profession. J. Am. Dent. Assoc. 131:1721-1728.
11. Fennell, J. F., W. H. Shipman, and L. J. Cole. 1967. Antibacterial action of a bee venom fraction (melittin) against a penicillin-resistant staphylococcus and other microorganisms, p. 1-25. U.S. Naval Radiological Defense Laboratory, Biological and Medical Sciences Division, San Francisco, CA.
12. Hancock, R. E. W., and D. S. Chapple. 1999. Peptide antibiotics. Antimicrob. Agents Chemother. 43:1317-1323.
13. Hancock, R. E. W., and R. Lehrer. 1998. Cationic peptides: a new source of antibiotics. Trends Biotechnol. 16:82-88. (Pubitemid 28055477)
14. He, J., et al. 2007. Novel synthetic antimicrobial peptides against Streptococcus mutans. Antimicrob. Agents Chemother. 51:1351-1358.
15. He, J., et al. 2010. Systematic approach to optimizing specifically targeted antimicrobial peptides against Streptococcus mutans. Antimicrob. Agents Chemother. 54:2143-2151.
16. He, X., R. Lux, H. K. Kuramitsu, M. H. Anderson, and W. Shi. 2009. Achieving probiotic effects via modulating oral microbial ecology. Adv. Dent. Res. 21:53-56.
17. Klocek, G., T. Schulthess, Y. Shai, and J. Seelig. 2009. Thermodynamics of melittin binding to lipid bilayers. Aggregation and pore formation. Biochemistry 48:2586-2596.
18. Kreth, J., Y. Zhang, and M. C. Herzberg. 2008. Streptococcal antagonism in oral biofilms: Streptococcus sanguinis and Streptococcus gordonii interference with Streptococcus mutans. J. Bacteriol. 190:4632-4640.
19. Kuramitsu, H. K., X. He, R. Lux, M. H. Anderson, and W. Shi. 2007. Interspecies interactions within oral microbial communities. Microbiol. Mol. Biol. Rev. 71:653-670.
20. Li, L., et al. 2010. Design and characterization of an acid-activated antimicrobial peptide. Chem. Biol. Drug Des. 75:127-132.
21. Li, L. N., et al. 2010. Targeted antimicrobial therapy against Streptococcus mutans establishes protective noncariogenic oral biofilms and reduces subsequent infection. Int. J. Oral Sci. 2:66-73.
22. Loesche, W. J. 1986. Role of Streptococcus mutans in human dental decay. Microbiol. Rev. 50:353-380.
23. Nakano, K., et al. 2009. Detection of oral bacteria in cardiovascular specimens. Oral Microbiol. Immunol. 24:64-68.
24. Oren, Z., and Y. Shai. 1998. Mode of action of linear amphipathic α-helical antimicrobial peptides. Biopolymers 47:451-463.
25. Oren, Z., and Y. Shai. 1997. Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: structure-function study. Biochemistry 36:1826-1835. (Pubitemid 27086279)
26. Parker, M. T., and L. C. Ball. 1976. Streptococci and aerococci associated with systemic infection in man. J. Med. Microbiol. 9:275-302.
27. Peschel, A., and H.-G. Sahl. 2006. The co-evolution of host cationic antimicrobial peptides and microbial resistance. Nat. Rev. Microbiol. 4:529-536.
28. Qi, F., et al. 2005. Peptide pheromone induced cell death of Streptococcus mutans. FEMS Microbiol. Lett. 251:321-326.
29. Rathinakumar, R., W. F. Walkenhorst, and W. C. Wimley. 2009. Broadspectrum antimicrobial peptides by rational combinatorial design and highthroughput screening: the importance of interfacial activity. J. Am. Chem. Soc. 131:7609-7617.
30. Sawai, M. V., et al. 2002. Impact of single-residue mutations on the structure and function of ovispirin/novispirin antimicrobial peptides. Protein Eng. 15:225-232. (Pubitemid 34429233)
31. Schüller, F., R. Benz, and H.-G. Sahl. 1989. The peptide antibiotic subtilin acts by formation of voltage-dependent multi-state pores in bacterial and artificial membranes. Eur. J. Biochem. 182:181-186.
32. Shai, Y. 1995. Molecular recognition between membrane-spanning polypeptides. Trends Biochem. Sci. 20:460-464.
33. Shin, S. Y., and K.-S. Hahm. 2004. A short α-helical antimicrobial peptide with antibacterial selectivity. Biotechnol. Lett. 26:735-739.
34. Sims, P. J., A. S. Waggoner, C. H. Wang, and J. F. Hoffman. 1974. Studies on the mechanism by which cyanine dyes measure membrane potential in red blood cells and phosphatidylcholine vesicles. Biochemistry 13:3315-3330.
35. Smith, R., et al. 1994. Structure and orientation of the pore-forming peptide melittin, in lipid bilayers. J. Mol. Biol. 241:456-466.
36. Tian, X., et al. 2009. A method for structure-activity analysis of quorum-sensing signaling peptides from naturally transformable streptococci. Biol. Proced. Online 11:207-226.
37. Tsang, P. W., et al. 2006. A medical approach to the diagnosis and treatment of dental caries. AHIP Cover. 47:38-42.
38. van den Bogaart, G., J. V. Guzmán, J. T. Mika, and B. Poolman. 2008. On the mechanism of pore formation by melittin. J. Biol. Chem. 283:33854-33857.
39. Woodworth, J. R., E. H. Nyhart, Jr., G. L. Brier, J. D. Wolny, and H. R. Black. 1992. Single-dose pharmacokinetics and antibacterial activity of daptomycin, a new lipopeptide antibiotic, in healthy volunteers. Antimicrob. Agents Chemother. 36:318-325.
40. Wu, M., E. Maier, R. Benz, and R. E. Hancock. 1999. Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli. Biochemistry 38:7235-7242.
41. Zendo, T., F. Yoneyama, and K. Sonomoto. 2010. Lactococcal membrane-permeabilizing antimicrobial peptides. Appl. Microbiol. Biotechnol. 88:1-9.