ArticleJournal of molecular biology2018
De Novo Designed α-Sheet Peptides Inhibit Functional Amyloid Formation of Streptococcus mutans Biofilms.
Article in Journal of molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 28 citations in OpenAlex.
- Serotype and distribution of adhesion genes in Streptococcus mutans isolated from people with Parkinson's disease.Odontology · 2025Article
- Designed De Novo α-Sheet Peptides Destabilize Bacterial Biofilms and Increase the Susceptibility ofInternational journal of molecular sciences · 2024Article
- Mechanistic insights into the role of amyloid-β in innate immunity.Scientific reports · 2024Article
- Designed α-sheet peptides disrupt uropathogenic E. coli biofilms rendering bacteria susceptible to antibiotics and immune cells.Scientific reports · 2023Article
- Gut Microbiota and Alzheimer's Disease: How to Study and Apply Their Relationship.International journal of molecular sciences · 2023Review
- 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
- Amyloid Aggregates Are Localized to the Nonadherent Detached Fraction of Aging Streptococcus mutans Biofilms.Microbiology spectrum · 2022Article
- Small molecule targeting amyloid fibrils inhibits Streptococcus mutans biofilm formation.AMB Express · 2021Article
- Roles and Mechanisms of Gut Microbiota in Patients With Alzheimer's Disease.Frontiers in aging neuroscience · 2021Review
- 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
- Enhanced purification coupled with biophysical analyses shows cross-β structure as a core building block for Streptococcus mutans functional amyloids.Scientific reports · 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
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Streptococcus mutans is a bacterial species that predominates in the oral microbiome. S. mutans binds to the tooth surface, metabolizes sugars and produces acid, leading to cavity formation. S. mutans can also cause infectious endocarditis. Recent evidence suggests that S. mutans biofilms contain amyloid fibrils. Amyloids are insoluble fibrillar protein aggregates, and bacteria use functional amyloids to improve robustness of their biofilms. While the functional amyloids in bacteria such as Escherichia coli and Staphylococcus aureus have been heavily investigated, little is known about the mechanism of S. mutans amyloid formation. Previous results from our laboratory with the amyloidogenic proteins and peptides from the aforementioned bacteria and other mammalian amyloid systems suggest that amyloid formation progresses via an intermediate that adopts a unique secondary structure-α-sheet. De novo designed peptides with alternating l- and d-amino acid also adopt an α-sheet secondary structure and inhibit amyloid formation by binding to soluble oligomeric species during amyloidogenesis. Inhibition of fibrillization by α-sheet peptides suggests the presence of α-sheet during amyloid formation. To investigate the mechanism of functional amyloid formation in S. mutans, α-sheet peptides were compared to epigallocatechin gallate for their ability to inhibit fibril formation in S. mutans. Inhibition was demonstrated in a biofilm plate assay and on hydroxyapatite surfaces both in S. mutans alone and in bacteria from human saliva. The observed inhibition suggests that an α-sheet mediated mechanism may be operative during functional amyloid formation.
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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.