ArticleAntibiotics (Basel, Switzerland)2023
D- and N-Methyl Amino Acids for Modulating the Therapeutic Properties of Antimicrobial Peptides and Lipopeptides.
Article in Antibiotics (Basel, Switzerland), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 15 citations in OpenAlex.
- Head-to-Tail Cyclization and D-Amino Acid Substitution Redesign the Biological Activities of a Naturally Occurring Amphibian Peptide.Molecules (Basel, Switzerland) · 2026Article
- Antimicrobial peptides for bacterial infections and their biomedical applications.Discover nano · 2026Review
- Structural Modification and Conjugation Strategies of Antimicrobial Peptides for Topical Anti-Infective Applications.Antibiotics (Basel, Switzerland) · 2026Review
- Lipopeptide Engineering: From Natural Origins to Rational Design Against Antimicrobial Resistance.Antibiotics (Basel, Switzerland) · 2026Review
- Systematic Determination of the Impact of Structural Edits on Peptide Accumulation into Mycobacteria.ACS chemical biology · 2025Article
- Expanding the genetic code: In vivo approaches for incorporating non-proteinogenic monomers.Journal of microbiology (Seoul, Korea) · 2025Review
- Recent Advances in Amphipathic Peptidomimetics as Antimicrobial Agents to Combat Drug Resistance.Molecules (Basel, Switzerland) · 2024Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
Abstract
Here we designed and synthesized analogs of two antimicrobial peptides, namely C10:0-A2, a lipopeptide, and TA4, a cationic α-helical amphipathic peptide, and used non-proteinogenic amino acids to improve their therapeutic properties. The physicochemical properties of these analogs were analyzed, including their retention time, hydrophobicity, and critical micelle concentration, as well as their antimicrobial activity against gram-positive and gram-negative bacteria and yeast. Our results showed that substitution with D- and N-methyl amino acids could be a useful strategy to modulate the therapeutic properties of antimicrobial peptides and lipopeptides, including enhancing stability against enzymatic degradation. The study provides insights into the design and optimization of antimicrobial peptides to achieve improved stability and therapeutic efficacy. TA4(dK), C10:0-A2(6-NMeLys), and C10:0-A2(9-NMeLys) were identified as the most promising molecules for further studies.
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Registered trials
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