The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Marine Antimicrobial Peptides: Nature Provides Templates for the Design of Novel Compounds against Pathogenic Bacteria
Open accessAbstract
The discovery of antibiotics for the treatment of bacterial infections brought the idea that bacteria would no longer endanger human health. However, bacterial diseases still represent a worldwide treat. The ability of microorganisms to develop resistance, together with the indiscriminate use of antibiotics, is mainly responsible for this situation; thus, resistance has compelled the scientific community to search for novel therapeutics. In this scenario, antimicrobial peptides (AMPs) provide a promising strategy against a wide array of pathogenic microorganisms, being able to act directly as antimicrobial agents but also being important regulators of the innate immune system. This review is an attempt to explore marine AMPs as a rich source of molecules with antimicrobial activity. In fact, the sea is poorly explored in terms of AMPs, but it represents a resource with plentiful antibacterial agents performing their role in a harsh environment. For the application of AMPs in the medical field limitations correlated to their peptide nature, their inactivation by environmental pH, presence of salts, proteases, or other components have to be solved. Thus, these peptides may act as templates for the design of more potent and less toxic compounds.
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Citations
Cites
Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
Brogden, K. A. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1098 · Cited by 5,829
Cationic Antimicrobial Peptides: Issues for Potential Clinical Use
Bradshaw, J. P. (2003) · BioDrugs · doi:10.2165/00063030-200317040-00002 · Cited by 293
Crustins: enigmatic WAP domain-containing antibacterial proteins from crustaceans
Smith, V. J., Fernandes, J. M. O., Kemp, G. D., & Hauton, C. (2008) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2007.12.002 · Cited by 281 · cited 1×
“Type III crustins lack the cysteine rich domain and glycine rich domain and contain a proline-arginine rich region together with the WAP domain [79].”
BackgroundCathelicidin family of antimicrobial peptides: Proteolytic processing and protease resistance
Shinnar, A. E., Butler, K. L., & Park, H. J. (2003) · Bioorganic Chemistry · doi:10.1016/s0045-2068(03)00080-4 · Cited by 170
Antimicrobial peptides: promising compounds against pathogenic microorganisms
Cruz, J., Ortiz, C., Guzmán, F., Fernández-Lafuente, R., & Torres, R. (2014) · Current Medicinal Chemistry · doi:10.2174/0929867321666140217110155 · Cited by 166
Membrane Activity of the Peptide Antibiotic Clavanin and the Importance of Its Glycine Residues
van Kan, E. J. M., van der Bent, A., Demel, R. A., & de Kruijff, B. (2001) · Biochemistry · doi:10.1021/bi0028136 · Cited by 52
Cited by
Sánchez, A., & Vázquez, A. (2017) · Food Quality and Safety · doi:10.1093/fqs/fyx006 · Cited by 868
Antimicrobial Peptides and Their Therapeutic Potential for Bacterial Skin Infections and Wounds
Pfalzgraff, A., Brandenburg, K., & Weindl, G. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.00281 · Cited by 481
Antimicrobial peptides (AMPs): A promising class of antimicrobial compounds
Erdem Büyükkiraz, M., & Kesmen, Z. (2022) · Journal of Applied Microbiology · doi:10.1111/jam.15314 · Cited by 454
Review: Lessons Learned From Clinical Trials Using Antimicrobial Peptides (AMPs)
Dijksteel, G. S., Ulrich, M. M. W., Middelkoop, E., & Boekema, B. K. H. L. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.616979 · Cited by 428
Hossain, T. J. (2024) · European Journal of Microbiology and Immunology · doi:10.1556/1886.2024.00035 · Cited by 392
Metadata
- Authors
- Falanga, A., Lombardi, L., Franci, G., Vitiello, M., Iovene, M., Morelli, G., Galdiero, M., & Galdiero, S.
- Venue
- International Journal of Molecular Sciences
- Publisher
- MDPI AG
- Published
- 2016-05-21
- Volume
- 17
- Issue
- 5
- Pages
- 785
- ISSN
- 1422-0067 (ISSN-L)
- OpenAlex
- W2406764016
- Cited by
- 164
- References
- 6
- FWCI
- 12.45
- Type
- journal article
- Language
- en
- Open access
- gold
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- Falanga, A., Lombardi, L., Franci, G., Vitiello, M., Iovene, M., Morelli, G., Galdiero, M., & Galdiero, S. (2016). Marine Antimicrobial Peptides: Nature Provides Templates for the Design of Novel Compounds against Pathogenic Bacteria. International Journal of Molecular Sciences. https://doi.org/10.3390/ijms17050785
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.