ArticleMolecules (Basel, Switzerland)2019
Peptide/Peptoid Hybrid Oligomers: The Influence of Hydrophobicity and Relative Side-Chain Length on Antibacterial Activity and Cell Selectivity.
Article in Molecules (Basel, Switzerland), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Recent progress in the structure-activity relationship of antibacterial peptoids.RSC advances · 2026Review
- Iterative discovery of potent polymeric antibiotics via multi-stage and multi-task learning against antimicrobial resistance.Nature communications · 2026Article
- Polymyxins with Potent Antibacterial Activity against Colistin-Resistant Pathogens: Fine-Tuning Hydrophobicity with Unnatural Amino Acids.Journal of medicinal chemistry · 2024Article
- Unnatural helical peptidic foldamers as protein segment mimics.Chemical Society reviews · 2023Review
- Disparate Regions of the Human Chemokine CXCL10 Exhibit Broad-Spectrum Antimicrobial Activity against Biodefense and Antibiotic-Resistant Bacterial Pathogens.ACS infectious diseases · 2023Article
- Article
- Hydrogen Bonding Drives Helical Chirality via 10-Membered Rings in Dipeptide Conjugates of Ferrocene-1,1'-Diamine.International journal of molecular sciences · 2022Article
- Macrocyclic Tetramers-Structural Investigation of Peptide-Peptoid Hybrids.Molecules (Basel, Switzerland) · 2021Article
- Peptide/β-Peptoid Hybrids with Ultrashort PEG-Like Moieties: Effects on Hydrophobicity, Antibacterial Activity and Hemolytic Properties.International journal of molecular sciences · 2021Article
- Peptide/β-Peptoid Hybrids with Activity against Vancomycin-Resistant Enterococci: Influence of Hydrophobicity and Structural Features on Antibacterial and Hemolytic Properties.International journal of molecular sciences · 2021Article
- The Potential of Modified and Multimeric Antimicrobial Peptide Materials as Superbug Killers.Frontiers in chemistry · 2021Review
- Halogenation as a tool to tune antimicrobial activity of peptoids.Scientific reports · 2020Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Previous optimisation studies of peptide/peptoid hybrids typically comprise comparison of structurally related analogues displaying different oligomer length and diverse side chains. The present work concerns a systematically constructed series of 16 closely related 12-mer oligomers with an alternating cationic/hydrophobic design, representing a wide range of hydrophobicity and differences in relative side-chain lengths. The aim was to explore and rationalise the structure-activity relationships within a subclass of oligomers displaying variation of three structural features: (i) cationic side-chain length, (ii) hydrophobic side-chain length, and (iii) type of residue that is of a flexible peptoid nature. Increased side-chain length of cationic residues led to reduced hydrophobicity till the side chains became more extended than the aromatic/hydrophobic side chains, at which point hydrophobicity increased slightly. Evaluation of antibacterial activity revealed that analogues with lowest hydrophobicity exhibited reduced activity against
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