ArticleNPJ biofilms and microbiomes2017
Designed α-sheet peptides suppress amyloid formation in
Article in NPJ biofilms and microbiomes, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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The trial behind it
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Who cites it
24 citing papers in PubMed.
- Targeting Eustachian Tube Microenvironment: Probiotic Surfactant Utilization for Antimicrobial Peptide Secretion to Prevent Otitis Media.Probiotics and antimicrobial proteins · 2026Review
- Layer-By-Layer Functionalized Gauze With Designed α-Sheet Peptides Inhibits E. coli and S. aureus Biofilm Formation.Journal of biomedical materials research. Part A · 2025Article
- Designed De Novo α-Sheet Peptides Destabilize Bacterial Biofilms and Increase the Susceptibility ofInternational journal of molecular sciences · 2024Article
- The role of shear rates on amyloid formation from biofilm peptide phenol-soluble modulins.Biophysical journal · 2024Article
- Human islet amyloid polypeptide-induced β-cell cytotoxicity is linked to formation of α-sheet structure.Protein science : a publication of the Protein Society · 2024Article
- Designed α-sheet peptides disrupt uropathogenic E. coli biofilms rendering bacteria susceptible to antibiotics and immune cells.Scientific reports · 2023Article
- SOBA: Development and testing of a soluble oligomer binding assay for detection of amyloidogenic toxic oligomers.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The role of α-sheet structure in amyloidogenesis: characterization and implications.Open biology · 2022Review
- Functional amyloids from bacterial biofilms - structural properties and interaction partners.Chemical science · 2022Review
- Cross-α/β polymorphism of PSMα3 fibrils.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Small molecule targeting amyloid fibrils inhibits Streptococcus mutans biofilm formation.AMB Express · 2021Article
- Anti-Biofilm Molecules Targeting Functional Amyloids.Antibiotics (Basel, Switzerland) · 2021Review
- Article
- Tumorigenic p53 mutants undergo common structural disruptions including conversion to α-sheet structure.Protein science : a publication of the Protein Society · 2020Article
- Self-targeting, zwitterionic micellar dispersants enhance antibiotic killing of infectious biofilms-An intravital imaging study in mice.Science advances · 2020Article
- Aggregation Mechanism of Alzheimer's Amyloid β-Peptide Mediated by α-Strand/α-Sheet Structure.International journal of molecular sciences · 2020Article
- Protein three-dimensional structures at the origin of life.Interface focus · 2019Review
- α-Sheet secondary structure in amyloid β-peptide drives aggregation and toxicity in Alzheimer's disease.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Anti-Biofilm Activity of Graphene Quantum Dots via Self-Assembly with Bacterial Amyloid Proteins.ACS nano · 2019Article
- Computational insights into the role of α-strand/sheet in aggregation of α-synuclein.Scientific reports · 2019Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Nosocomial infections affect hundreds of millions of patients worldwide each year, and ~60% of these infections are associated with biofilm formation on an implanted medical device. Biofilms are dense communities of microorganisms in which cells associate with surfaces and each other using a self-produced extracellular matrix composed of proteins, polysaccharides, and genetic material. Proteins in the extracellular matrix take on a variety of forms, but here we focus on functional amyloid structures. Amyloids have long been associated with protein misfolding and neurodegenerative diseases, but recent research has demonstrated that numerous bacterial species utilize the amyloid fold to fortify the biofilm matrix and resist disassembly. Consequently, these functional amyloids, in particular the soluble oligomeric intermediates formed during amyloidogenesis, represent targets to destabilize the extracellular matrix and interrupt biofilm formation. Our previous studies suggested that these amyloidogenic intermediates adopt a non-standard structure, termed "α-sheet", as they aggregate into soluble oligomeric species. This led to the design of complementary α-sheet peptides as anti-α-sheet inhibitors; these designs inhibit amyloidogenesis in three unrelated mammalian disease-associated systems through preferential binding of soluble oligomers. Here we show that these anti-α-sheet peptides inhibit amyloid formation in
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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.