ArticleACS omega2021
Tuning the Activity of Anoplin by Dendrimerization of Lysine and Lipidation of the N-Terminal.
Article in ACS omega, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed.
- Article
- Impact of Lysine-Mediated C-Terminal Dimerization of Anoplin on Killing Kinetics and Antibiotic Interaction Profiles.Microorganisms · 2026Article
- Therapeutic peptides: chemical strategies fortify peptides for enhanced disease treatment efficacy.Amino acids · 2025Review
- Antibacterial and Anti-Inflammatory Activity of Branched Peptides Derived from Natural Host Defense Sequences.Journal of medicinal chemistry · 2024Article
- The Potential of Modified and Multimeric Antimicrobial Peptide Materials as Superbug Killers.Frontiers in chemistry · 2021Review
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dendrimeric antimicrobial peptides or lipopeptides have strong transmembrane ability and antibacterial activity. To obtain some ideal antimicrobial peptides, anoplin, a natural antimicrobial peptide with weak antimicrobial activity, was modified by C-terminal dendrimerization using lysine and N-terminal lipidation using fatty acids. 2K-3A-C4, a trimer of anoplin, was dendrimerized by two lysines at the C-terminal and was lipidated by
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Registered trials
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