ArticleNature chemical biology2025
Rapid discovery of cyclic peptide protein aggregation inhibitors by continuous selection.
Article in Nature chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed.
- De Novo Discovery of Bioactive Cyclic Peptides via Cellular Selection of Genetically Encoded Libraries.Chembiochem : a European journal of chemical biology · 2026Review
- Bridging Heterocycle-Mediated Hydrogen Bonding Facilitates Permeability of Polar Macrobicycles.Journal of the American Chemical Society · 2026Article
- Identification of Secondary Nucleation Inhibitors of Amyloid-β Aggregation by Cellular Selection of a SICLOPPS Library.Chembiochem : a European journal of chemical biology · 2026Article
- From Gene Knockouts to Genome Remodeling: Large DNA Fragment Deletion Technologies in Plants.Plants (Basel, Switzerland) · 2026Review
- Universal Baseline forbioRxiv : the preprint server for biology · 2026Article
- De novo cyclic peptides allow visualisation of the monomeric and functional amyloid conformations of the kinase RIPK3.The Biochemical journal · 2026Article
- Phage-Assisted Continuous Selection of Bioactive Cyclic Peptides.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Boosting Quantification of N-Glycans by an Enhanced Isobaric Multiplex Reagents for Carbonyl-Containing Compound (SUGAR) Tagging Strategy.Journal of the American Society for Mass Spectrometry · 2025Article
- Antiparallel β-Sheet as a Key Motif of Amyloid-β Inhibitor Designed via Topological Peptide Reprogramming.Angewandte Chemie (International ed. in English) · 2025Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Protein aggregates are associated with numerous diseases. Here we report a platform for the rapid phenotypic selection of protein aggregation inhibitors from genetically encoded cyclic peptide libraries in Escherichia coli based on phage-assisted continuous evolution (PACE). We developed a new PACE-compatible selection for protein aggregation inhibition and used it to identify cyclic peptides that suppress amyloid-β42 and human islet amyloid polypeptide aggregation. Additionally, we integrated a negative selection that removes false positives and off-target hits, greatly improving cyclic peptide selectivity. We show that selected inhibitors are active when chemically resynthesized in in vitro assays. Our platform provides a powerful approach for the rapid discovery of cyclic peptide inhibitors of protein aggregation and may serve as the basis for the future evolution of cyclic peptides with a broad spectrum of inhibitory activities.
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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.