The Road from Host-Defense Peptides to a New Generation of Antimicrobial Drugs
Open accessAbstract
Host-defense peptides, also called antimicrobial peptides (AMPs), whose protective action has been used by animals for millions of years, fulfill many requirements of the pharmaceutical industry, such as: (1) broad spectrum of activity; (2) unlike classic antibiotics, they induce very little resistance; (3) they act synergically with conventional antibiotics; (4) they neutralize endotoxins and are active in animal models. However, it is considered that many natural peptides are not suitable for drug development due to stability and biodisponibility problems, or high production costs. This review describes the efforts to overcome these problems and develop new antimicrobial drugs from these peptides or inspired by them. The discovery process of natural AMPs is discussed, as well as the development of synthetic analogs with improved pharmacological properties. The production of these compounds at acceptable costs, using different chemical and biotechnological methods, is also commented. Once these challenges are overcome, a new generation of versatile, potent and long-lasting antimicrobial drugs is expected.
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AMPs are an important component of the innate immune system in all organisms, including plants, animals, and humans, providing a rapid and non-specific response to pathogens.
“Antimicrobial peptides AMPs are an important component of the innate immune system in all organisms, including plants, animals, and humans, providing a rapid and non-specific response to pathogens [175].”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [175]
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References 149 · Cited by 136
Research works printed but not linked: 8
- [2]Handbook of Biologically Active Peptides Kastin A.J. Academic Press San Diego, CA, USA 2006
- [7]This review does not cover other antimicrobial peptides (such as valinomycin) which do not meet these structural requirements to resemble host-defense peptides.
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- [38]For On-Line Information on Gramicidins Available online: https://pubchem.ncbi.nlm.nih.gov/compound/gramicidin (accessed on 16 January 2018)
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- Authors
- Boto, A., Pérez de la Lastra, J., & González, C.
- Affiliations
- Instituto de Productos Naturales y Agrobiología (ES)
- Instituto de Productos Naturales y Agrobiología del CSIC, CSIC-Spanish Research Council, Avda. Astrofísico Fco. Sánchez, 3-38206 La Laguna, Tenerife, Spain
- Corresponding author
- Boto, Alicia
- Venue
- Molecules
- Publisher
- MDPI AG
- Published
- 2018-02-01
- Volume
- 23
- Issue
- 2
- Pages
- 311
- ISSN
- 1420-3049 (ISSN-L)
- PMC
- PMC6017364
- OpenAlex
- W2791018471
- Cited by
- 136
- References
- 149
- Citations by year
- 2026: 8 · 2025: 13 · 2024: 16 · 2023: 13 · 2022: 20 · 2021: 20 · 2020: 20 · 2019: 16 · 2018: 7 · 2017: 1
- FWCI
- 2.24
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Molecules (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DIGITAL.CSIC (Spanish National Research Council (CSIC)) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Ministerio de Asuntos Económicos y Transformación Digital, Gobierno de España
- Topics
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Physical Sciences › Chemistry › Organic Chemistry › Antimicrobial agents and applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
- Keywords
- antimicrobial peptides, antimicrobial drug development, synthetic peptide analogs, peptide stability, bioavailability, antibiotic resistance, endotoxin neutralization, peptide discovery, peptide production
- MeSH terms
- Paenibacillus polymyxa, Protein Conformation, alpha-Helical, Protein Conformation, beta-Strand, Animals, Anti-Infective Agents, Humans, Polymyxins, Structure-Activity Relationship, Drug Design, Antimicrobial Cationic Peptides, Hydrophobic and Hydrophilic Interactions
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