The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Antimicrobial peptides: an overview of a promising class of therapeutics
Open accessAbstract
Antibiotic resistance is increasing at a rate that far exceeds the pace of new development of drugs. Antimicrobial peptides, both synthetic and from natural sources, have raised interest as pathogens become resistant against conventional antibiotics. Indeed, one of the major strengths of this class of molecules is their ability to kill multidrug-resistant bacteria. Antimicrobial peptides are relatively small (6 to 100 aminoacids), amphipathic molecules of variable length, sequence and structure with activity against a wide range of microorganisms including bacteria, protozoa, yeast, fungi, viruses and even tumor cells. They usually act through relatively non-specific mechanisms resulting in membranolytic activity but they can also stimulate the innate immune response. Several peptides have already entered pre-clinical and clinical trials for the treatment of catheter site infections, cystic fibrosis, acne, wound healing and patients undergoing stem cell transplantation. We review the advantages of these molecules in clinical applications, their disadvantages including their low in vivo stability, high costs of production and the strategies for their discovery and optimization.
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Cites
Antimicrobial peptides of multicellular organisms
Zasloff, M. (2002) · Nature · doi:10.1038/415389a · Cited by 8,457
Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
Brogden, K. A. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1098 · Cited by 5,829
β-Defensins: Linking Innate and Adaptive Immunity Through Dendritic and T Cell CCR6
Yang, D., Chertov, O., Bykovskaia, S. N., Chen, Q., Buffo, M. J., Shogan, J., Anderson, M., Schröder, J. M., Wang, J. M., Howard, O. M. Z., et al. (1999) · Science · doi:10.1126/science.286.5439.525 · Cited by 1,809
Tam, J. P. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.15.5409 · Cited by 1,251 · cited 1×
“Multiple antigen peptide (MAP), consisting of a number of peptides covalently attached to a branching lysine core (Figure 2), was originally developed by Tam as a peptidic immunogen for preparation of antibody [139].”
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Cited by
A New Era of Antibiotics: The Clinical Potential of Antimicrobial Peptides
Browne, K., Chakraborty, S., Chen, R., Willcox, M. D., Black, D. S., Walsh, W. R., & Kumar, N. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197047 · Cited by 482
CAMP: a useful resource for research on antimicrobial peptides.
Thomas, S., Karnik, S., Barai, R. S., Jayaraman, V. K., & Idicula-Thomas, S. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkp1021 · Cited by 462
Antimicrobial Peptides: Primeval Molecules or Future Drugs?
Peters, B. M., Shirtliff, M. E., & Jabra-Rizk, M. A. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1001067 · Cited by 425
Antimicrobial peptides: Structure, mechanism, and modification
Chen, N., & Jiang, C. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115377 · Cited by 279
Structure–activity relationship of cationic surfactants as antimicrobial agents
Zhou, C., & Wang, Y. (2020) · Current Opinion in Colloid & Interface Science · doi:10.1016/j.cocis.2019.11.009 · Cited by 258
Metadata
- Authors
- Giuliani, A., Pirri, G., & Nicoletto, S.
- Venue
- Open Life Sciences
- Publisher
- Walter de Gruyter GmbH
- Published
- 2007-03-01
- Volume
- 2
- Issue
- 1
- Pages
- 1-33
- ISSN
- 1895-104X (ISSN-L)
- 2391-5412
- OpenAlex
- W2059884070
- Cited by
- 606
- References
- 4
- FWCI
- 16.07
- Type
- journal article
- Language
- en
- Open access
- hybrid
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