ArticleFEBS letters2016
Hairpin structure stability plays a role in the activity of two antimicrobial peptides.
Article in FEBS letters, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers, 1 of them a synthesis that pooled it.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
8 citing papers in PubMed, 1 synthesis or guideline pooled it, 20 citations in OpenAlex.
- Peptide Designs for Use in Caries Management: A Systematic Review.International journal of molecular sciences · 2023Pooled it
- The rise and future of peptide-based antimicrobials.Journal of microbiology (Seoul, Korea) · 2026Review
- Turn-engineering tunes the conformational rigidity of β-hairpin AMPs in achieving membrane selectivity and killing drug-resistant ESKAPE pathogens.Chemical science · 2025Article
- Small Natural Cyclic Peptides from DBAASP Database.Pharmaceuticals (Basel, Switzerland) · 2024Review
- Molecular Dynamics Study of Citrullinated Proteins Associated with the Development of Rheumatoid Arthritis.Proteomes · 2022Article
- A systematic analysis of the beta hairpin motif in the Protein Data Bank.Protein science : a publication of the Protein Society · 2021Article
- β-Turn Mimics by Chemical Ligation.Organic letters · 2020Article
- Biological consequences of improving the structural stability of hairpins that have antimicrobial activity.Journal of peptide science : an official publication of the European Peptide Society · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Many naturally occurring antimicrobial peptides (AMPs) are amphipathic with a β-hairpin conformation stabilized by cross-strand disulfides across the associated β-strands. Here, we show that the disulfides are not essential. Other structuring means such as better β-turns and noncovalent cross-strand interactions can, with proper design, replace the disulfides with no loss in antimicrobial activity. Our results also demonstrate that the hairpin turn region may play a role in membrane recognition for at least one member of this class, since a homodimeric turnless β-sheet analog showed no antimicrobial activity. We also examined the effects of N-terminal fatty acid adducts on AMPs. Surprisingly, the large hydrophobic carboxylic moieties examined completely eliminated the antimicrobial activity of previously active β-hairpin peptides.
Indexed as
Identifiers
What OpenQuestion holds
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.