Perspectives for clinical use of engineered human host defense antimicrobial peptides
Open accessAbstract
Infectious diseases caused by bacteria, viruses or fungi are among the leading causes of death worldwide. The emergence of drug-resistance mechanisms, especially among bacteria, threatens the efficacy of all current antimicrobial agents, some of them already ineffective. As a result, there is an urgent need for new antimicrobial drugs. Host defense antimicrobial peptides (HDPs) are natural occurring and well-conserved peptides of innate immunity, broadly active against Gram-negative and Gram-positive bacteria, viruses and fungi. They also are able to exert immunomodulatory and adjuvant functions by acting as chemotactic for immune cells, and inducing cytokines and chemokines secretion. Moreover, they show low propensity to elicit microbial adaptation, probably because of their non-specific mechanism of action, and are able to neutralize exotoxins and endotoxins. HDPs have the potential to be a great source of novel antimicrobial agents. The goal of this review is to provide an overview of the advances made in the development of human defensins as well as the cathelicidin LL-37 and their derivatives as antimicrobial agents against bacteria, viruses and fungi for clinical use.
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LL-37 is considered an ideal template or molecular skeleton for the development of new antimicrobial drugs.
“For this reason, LL-37 is considered an ideal template or a molecular skeleton for the development of new antimicrobial drugs.36”
From Identification of heptapeptides targeting a lethal bacterial strain in septic mice through an integrative approach (2022) · cites this paper as [36]
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“For this reason, LL-37 is considered an ideal template or a molecular skeleton for the development of new antimicrobial drugs.(36)”
Background
- Authors
- Pachón-Ibáñez, M. E., Smani, Y., Pachón, J., & Sánchez-Céspedes, J.
- Affiliations
- Consejo Superior de Investigaciones Científicas (ES)
- Corresponding author
- Pachón-Ibáñez, María Eugenia
- Smani, Younes
- Venue
- FEMS Microbiology Reviews
- Publisher
- Oxford University Press (OUP)
- Published
- 2017-05-01
- Volume
- 41
- Issue
- 3
- Pages
- 323-342
- ISSN
- 0168-6445 (ISSN-L)
- 1574-6976
- PMC
- PMC5435762
- OpenAlex
- W2616486904
- Cited by
- 159
- References
- 5
- Citations by year
- 2026: 10 · 2025: 15 · 2024: 15 · 2023: 15 · 2022: 23 · 2021: 17 · 2020: 24 · 2019: 24 · 2018: 13 · 2017: 3
- FWCI
- 2.50
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-nd
- Locations
- FEMS Microbiology Reviews (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- DIGITAL.CSIC (Spanish National Research Council (CSIC)) (submittedVersion, cc-by-nc-nd)
- RISalud Institutional Health Repository of Andalucía (submittedVersion, cc-by-nc-nd)
- Funders
- Spanish Network for Research in Infectious Diseases (REIPI RD12/0015/0001, REIPI RD16/0009)
- Topics
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Physical Sciences › Chemistry › Organic Chemistry › Antimicrobial agents and applications
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Keywords
- human defensins, cathelicidin LL-37, antimicrobial resistance, innate immunity, immunomodulation, antiviral activity, antifungal activity, clinical application, endotoxin neutralization
- MeSH terms
- Anti-Infective Agents, Bacteria, Bacterial Infections, Endotoxins, Exotoxins, Fungi, Humans, Microbial Sensitivity Tests, Mycoses, Virus Diseases, Viruses, Defensins, Antimicrobial Cationic Peptides, Cathelicidins
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