Skip to main content
Log in

Host Defence (bdCationic) Peptides

What Is Their Future Clinical Potential?

  • Leading Article
  • Published:
Drugs Aims and scope Submit manuscript

Abstract

Host defence, cationic antimicrobial peptides are now recognised as an important component, in most species, of the early innate and induced defences against invading microbes. They are small (12 to 35 amino acids), cationic due to the presence of an excess of arginine and lysine over acidic amino acids, and able to fold into a variety of different secondary structures. They have highly desirable properties, such as the ability to kill rapidly a broad spectrum of microorganisms including drug resistant bacteria and often fungi at around the minimal inhibitory concentration, a low level of resistance development in vitro, the ability to protect animals against both topical and systemic infections and the capability to neutralise endotoxin and demonstrated synergy with conventional antibiotics. In addition, given the 20 building blocks (amino acids) for these peptides, even a small peptide offers enormous diversity and potential for design of improved variants. For this reason such peptides have entered clinical trials, largely as agents for topical therapy of polymicrobial infections and are considered to have excellent potential for being a novel antibiotic class.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  1. Boman HG. Peptide antibiotics and their role in innate immunity. Annu Rev Immunol 1995; 13: 61–92

    Article  PubMed  CAS  Google Scholar 

  2. Ganz T, Lehrer RI. Antimicrobial peptides of leukocytes. Curr Opin Hematol 1997; 4: 53–8

    Article  PubMed  CAS  Google Scholar 

  3. Hancock REW, Falla T, Brown MM. Cationic bactericidal peptides. Adv Microb Physiol 1995; 37: 135–75

    Article  PubMed  CAS  Google Scholar 

  4. Hancock REW, Lehrer RI. Cationic peptides: a new source of antibiotics. Trends Biotech 1998; 16: 82–8

    Article  CAS  Google Scholar 

  5. Kadalayil L, Petersen UM, Engstrom Y. Adjacent GATA and Kappa β-like motifs regulate the expression of a Drosophila immune gene. Nucl Acids Res 1997; 25: 1233–9

    Article  PubMed  CAS  Google Scholar 

  6. Hancock REW. Peptide antibiotics. Lancet 1997; 349: 418–22

    Article  PubMed  CAS  Google Scholar 

  7. Steinberg DA, Hurst MA, Fujii CA, et al. Protegrin-1: a broad spectrum, rapidly microbicidal peptide with in vivo activity. Antimicrob Agents Chemother 1997; 41: 1738–42

    PubMed  CAS  Google Scholar 

  8. Kondejewski LH, Fanner SW, Wishart DS, et al. Gramicidin S is active against both gram-positive and gram-negative bacteria. Int J Peptein Prot Res 1996; 47: 460–6

    Article  CAS  Google Scholar 

  9. Gough M, Hancock REW, Kelly NM. Anti-endotoxic potential of cationic peptide antimicrobials. Infect Immun 1996; 64: 4922–7

    PubMed  CAS  Google Scholar 

  10. Hancock REW. Therapeutic potential of cationic peptides. Expert Opin Invest Dis 1998; 7: 167–74

    Article  CAS  Google Scholar 

  11. Darveau RP, Cunningham MD, Seaford CL, et al. Beta-lactam antibiotics potentiate magainin 2 antimicrobial activity in vitro and in vivo. Antimicrob Agents Chemother 1991; 35: 1153–9

    Article  PubMed  CAS  Google Scholar 

  12. Rogy MA, Oldenburg HSA, Calvano SE, et al. The role of bactericidal/permeability-increasing protein in the treatment of primate bacteremia and septic shock. J Clin Immunol 1994; 14: 120–33

    Article  PubMed  CAS  Google Scholar 

  13. Appenzeller L, Lim E, Wong P, et al. In vivo fungicidal activity of optimized domain III peptides derived from bactericidal/ permeability-increasing protein BPI [abstract F187]. 36th International Conference on Antimicrobial Agents and Chemotherapy: 1996 Sep 17–20; New Orleans, 132

  14. Nakashima H, Masuda M, Murakami T, et al. Anti-human immunodeficiency virus activity of a novel synthetic peptide, T22 ([Tyr-5,12, Lys-7] Polyphemusin II): a possible inhibitor of virus-cell fusion. Antimicrob Agents Chemother 1992; 36: 1249–55

    Article  PubMed  CAS  Google Scholar 

  15. Rodriguez MC, Zamudio F, Torres JA, et al. Effect of a cecropin-like synthetic peptide (Shiva -3) on the sporogenic development of Plasmodium berghei. Exp Parasitai 1995; 80: 596–604

    Article  CAS  Google Scholar 

  16. Sawyer JG, Martin NL, Hancock REW. Interaction of macrophage cationic proteins with the outer membrane of Pseudomonas aeruginosa. Infect Immun 1988; 56: 693–8

    PubMed  CAS  Google Scholar 

  17. Moore AJ, Devine DA, Bibby MC. Preliminary experimental anti-cancer activity of cecropin B. Peptide Res 1994; 7: 265–9

    CAS  Google Scholar 

  18. D’Cruz OJ, Periera A, Haas GG. Sperm immobilizing activity of a synthetic bioactive peptide 20–44 of 37-kDa cationic antimicrobial protein (CAP37) of human neutrophils. J Androl 1995; 16: 432–40

    PubMed  Google Scholar 

  19. Jensen T, Pedersen SS, Garne S, et al. Colistin inhalation therapy in cystic fibrosis patients with chronic Pseudomonas aeruginosa lung infection. J Antimicrob Chemother 1987; 19: 831–8

    Article  PubMed  CAS  Google Scholar 

  20. Ahmad I, Perkins WR, Lupan DM, et al. Liposomal entrapment of the neutrophil-derived peptide indolicidin endows it with in vivo antifungal activity. Biochim Biophys Acta 1995; 1237: 109–14

    Article  PubMed  Google Scholar 

  21. Piers KL, Brown MH, Hancock REW. Recombinant DNA procedures for producing small antimicrobial cationic peptides in bacteria. Gene 1993; 134: 7–13

    Article  PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Robert E. W. Hancock.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Hancock, R.E.W. Host Defence (bdCationic) Peptides. Drugs 57, 469–473 (1999). https://doi.org/10.2165/00003495-199957040-00002

Download citation

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.2165/00003495-199957040-00002

Keywords

Navigation