ArticleiScience2022
Synthetic antibacterial discovery of symbah-1, a macrocyclic β-hairpin peptide antibiotic.
Article in iScience, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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.
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Who cites it
10 citing papers in PubMed.
- AI-Driven Discovery and Design of Antimicrobial Peptides: Progress, Challenges, and Opportunities.Probiotics and antimicrobial proteins · 2026Review
- β-Hairpin Antimicrobial Peptides: Class Diversity and Sequence Analysis.ACS infectious diseases · 2026Review
- Inter- and intra-bacterial strain diversity remains the "elephant in the (living) room".npj antimicrobials and resistance · 2025Review
- Deep mutational scanning and machine learning for the analysis of antimicrobial-peptide features driving membrane selectivity.Nature biomedical engineering · 2024Article
- Development of a Selective and Stable Antimicrobial Peptide.ACS infectious diseases · 2024Article
- Alternative therapeutic strategies to treat antibiotic-resistant pathogens.Nature reviews. Microbiology · 2024Review
- Adapting antibacterial display to identify serum-active macrocyclic peptide antibiotics.PNAS nexus · 2023Article
- Adapting antibacterial display to identify serum active macrocyclic peptide antibiotics.bioRxiv : the preprint server for biology · 2023Article
- Using display technologies to identify macrocyclic peptide antibiotics.Biochimica et biophysica acta. Molecular cell research · 2023Review
- Designing and identifying β-hairpin peptide macrocycles with antibiotic potential.Science advances · 2023Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
The rapid development and spread of antibiotic resistance necessitate the development of novel strategies for antibiotic discovery. Symbah-1, a synthetic peptide antibiotic, was identified in a high-throughput antibacterial screen of random peptide sequences. Symbah-1 functions through membrane disruption and contains broad spectrum bactericidal activity against several drug-resistant pathogens. Circular dichroism and high-resolution mass spectrometry indicate symbah-1 has a β-hairpin structure induced by lipopolysaccharide and is cyclized via an intramolecular disulfide bond. Together these data classify symbah-1 as an uncommon synthetic member of the β-hairpin antimicrobial peptide class. Symbah-1 displays low hemolysis but loses activity in human serum. Characterization of a symbah-1 peptide library identified two variants with increased serum activity and protease resistance. The method of discovery and subsequent characterization of symbah-1 suggests large synthetic peptide libraries bias toward macrocyclic β-hairpin structure could be designed and screened to rapidly expand and better understand this rare peptide antibiotic class.
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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.