ArticleScientific reports2018
Exploring the role of unnatural amino acids in antimicrobial peptides.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 106 citations in OpenAlex.
- Design, synthesis, molecular docking, and antimicrobial evaluation of hybrid peptides incorporating unnatural amino acids with enhanced hydrophobic sidechains.RSC advances · 2026Article
- Optimization strategies for antimicrobial peptides in dental caries prevention and management: from emerging mechanisms of action to clinical translation.Frontiers in microbiology · 2026Review
- Dual-action thioarylamide-based small molecules to target drug-resistant bacteria and chronic inflammation.iScience · 2025Article
- Serendipitous Hinge Modulation Hypothetically Reprograms Caerin 1.1-LC Antibacterial Mechanism and Gram-Negative Selectivity.Pharmaceutics · 2025Article
- Deep-Learning Driven Identification of Novel Antimicrobial Peptides.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Molecular Dynamics (MD)-Derived Features for Canonical and Noncanonical Amino Acids.Journal of chemical information and modeling · 2025Article
- Unlocking the power of antimicrobial peptides: advances in production, optimization, and therapeutics.Frontiers in cellular and infection microbiology · 2025Review
- How Unnatural Amino Acids in Antimicrobial Peptides Change Interactions with Lipid Model Membranes.The journal of physical chemistry. B · 2024Article
- Peptide-based drug discovery through artificial intelligence: towards an autonomous design of therapeutic peptides.Briefings in bioinformatics · 2024Review
- Hydrolysis of Antimicrobial Peptides by Extracellular Peptidases in Wastewater.Environmental science & technology · 2024Article
- Sequence-based prediction of the intrinsic solubility of peptides containing non-natural amino acids.Nature communications · 2023Article
- Self-Entrapment of Antimicrobial Peptides in Silica Particles for Stable and Effective Antimicrobial Peptide Delivery System.International journal of molecular sciences · 2023Article
- Molecular hybridization strategy for tuning bioactive peptide function.Communications biology · 2023Article
- Modified CLEC3A-Derived Antimicrobial Peptides Lead to Enhanced Antimicrobial Activity against Drug-Resistant Bacteria.Antibiotics (Basel, Switzerland) · 2023Article
- Combining the Peptide RWQWRWQWR and an Ethanolic Extract ofJournal of fungi (Basel, Switzerland) · 2023Article
- Inhibitory Potential of Synthetic Amino Acid Derivatives against Digestive Enzymes as Promising Hypoglycemic and Anti-Obesity Agents.Biomolecules · 2023Article
- Antibacterial Activity and Mechanisms of TroHepc2-22, a Derived Peptide of Hepcidin2 from Golden Pompano (International journal of molecular sciences · 2023Article
- The impact of N-glycosylation on the properties of the antimicrobial peptide LL-III.Scientific reports · 2023Article
- Article
- Synergistic effect and antibiofilm activity of the antimicrobial peptide K11 with conventional antibiotics against multidrug-resistant and extensively drug-resistantFrontiers in cellular and infection microbiology · 2023Article
Corrections and comments
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Authors and funding
13 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cationic antimicrobial peptides (CAMPs) are a promising alternative to treat multidrug-resistant bacteria, which have developed resistance to all the commonly used antimicrobial, and therefore represent a serious threat to human health. One of the major drawbacks of CAMPs is their sensitivity to proteases, which drastically limits their half-life. Here we describe the design and synthesis of three nine-residue CAMPs, which showed high stability in serum and broad spectrum antimicrobial activity. As for all peptides a very low selectivity between bacterial and eukaryotic cells was observed, we performed a detailed biophysical characterization of the interaction of one of these peptides with liposomes mimicking bacterial and eukaryotic membranes. Our results show a surface binding on the DPPC/DPPG vesicles, coupled with lipid domain formation, and, above a threshold concentration, a deep insertion into the bilayer hydrophobic core. On the contrary, mainly surface binding of the peptide on the DPPC bilayer was observed. These observed differences in the peptide interaction with the two model membranes suggest a divergence in the mechanisms responsible for the antimicrobial activity and for the observed high toxicity toward mammalian cell lines. These results could represent an important contribution to unravel some open and unresolved issues in the development of synthetic CAMPs.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.