Triazole-Bridged Peptides with Enhanced Antimicrobial Activity and Potency against Pathogenic Bacteria
Open accessAbstract
There are still no linear antimicrobial peptides (AMPs) available as a treatment option against bacterial infections. This is caused by several drawbacks that come with AMPs such as limited proteolytic stability and low selectivity against human cells. In this work, we screened a small library of rationally designed new peptides based on the cell-penetrating peptide sC18* toward their antimicrobial activity. We identified several effective novel AMPs and chose one out of this group to further increase its potency. Therefore, we introduced a triazole bridge at different positions to provide a preformed helical structure, assuming that this modification would improve (i) proteolytic stability and (ii) membrane activity. Indeed, placing the triazole bridge within the hydrophilic part of the linear analogue highly increased membrane activity as well as stability against enzymatic digestion. The new peptides, 8A and 8B, demonstrated high activity against several bacterial species tested including pathogenic N. gonorrhoeae and methicillin-resistant S. aureus . Since they exhibited significantly good tolerability against human fibroblast and blood cells, these novel peptides offer true alternatives for future clinical applications and are worth studying in more detail.
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Research works printed but not linked: 1
- Antonie van Leeuwenhoek, Int. J. Gen. Mol. Microbiol. 2020, 113 (1), 1- 12.
Cited by
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Varró, N., Mándityné Huszka, B., Erdei, E., Mándoki, A., & Mándity, I. M. (2025) · Chemistry–Methods · doi:10.1002/cmtd.202500010 · Cited by 8 · see citing works
- Authors
- Grabeck, J., Mayer, J., Miltz, A., Casoria, M., Quagliata, M., Meinberger, D., Klatt, A. R., Wielert, I., Maier, B., Papini, A. M., & Neundorf, I.
- Affiliations
- University of Cologne (DE)
- University of Florence (IT)
- Corresponding author
- Neundorf, Ines
- ORCID
- Venue
- ACS Infectious Diseases
- Publisher
- American Chemical Society (ACS)
- Published
- 2024-06-17
- Volume
- 10
- Issue
- 8
- Pages
- 2717-2727
- ISSN
- 2373-8227 (ISSN-L)
- OpenAlex
- W4399723120
- Cited by
- 7
- References
- 38
- Citations by year
- 2026: 1 · 2025: 6
- FWCI
- 1.81
- Type
- journal article
- Language
- en
- Open access
- green
- pubs.acs.org
- Licence
- Locations
- ACS Infectious Diseases (publishedVersion)
- PubMed (publishedVersion)
- Florence Research (University of Florence) (submittedVersion, other-oa)
- Funders
- Deutsche Forschungsgemeinschaft (NE14-10)
- EUniWell
- Erasmus+ exchange program
- 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, peptide library screening, proteolytic stability, membrane activity, Neisseria gonorrhoeae, methicillin-resistant Staphylococcus aureus, antibacterial activity, rational peptide design
- MeSH terms
- Antimicrobial Peptides, Anti-Bacterial Agents, Bacteria, Fibroblasts, Humans, Microbial Sensitivity Tests, Neisseria gonorrhoeae, Triazoles, Methicillin-Resistant Staphylococcus aureus
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