ArticleMicrobial biotechnology2021
The broad-spectrum antibiofilm activity of amyloid-forming hexapeptides.
Article in Microbial biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 18 citations in OpenAlex.
- Optimization strategies for antimicrobial peptides in dental caries prevention and management: from emerging mechanisms of action to clinical translation.Frontiers in microbiology · 2026Review
- Antimicrobial Peptides as Novel Ecological Approaches to Caries Prevention.Drug design, development and therapy · 2026Review
- Synergistic inhibition ofFrontiers in microbiology · 2026Article
- From Pathology to Materials Science and Engineering: Harnessing the Amyloid State for Biotechnological Applications.ACS applied materials & interfaces · 2025Review
- Computational-aided drug design strategies for drug discovery and development against oral diseases.Frontiers in pharmacology · 2025Review
- Designed De Novo α-Sheet Peptides Destabilize Bacterial Biofilms and Increase the Susceptibility ofInternational journal of molecular sciences · 2024Article
- Amyloid peptides with antimicrobial and/or microbial agglutination activity.Applied microbiology and biotechnology · 2022Review
- Comparative Study of the Solid-Liquid Interfacial Adsorption of Proteins in Their Native and Amyloid Forms.International journal of molecular sciences · 2022Article
- Amyloidogenic Peptides: New Class of Antimicrobial Peptides with the Novel Mechanism of Activity.International journal of molecular sciences · 2022Review
- Small molecule targeting amyloid fibrils inhibits Streptococcus mutans biofilm formation.AMB Express · 2021Article
- Anti-Biofilm Molecules Targeting Functional Amyloids.Antibiotics (Basel, Switzerland) · 2021Review
- The broad-spectrum antibiofilm activity of amyloid-forming hexapeptides.Microbial biotechnology · 2021Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Evidence suggests that short amyloid-forming peptides derived from bacterial proteomes have functional roles; however, the reported activities are diverse and the underlying mechanisms remain unclear. In this study, we simulated short amyloid-forming peptides from the amyloid-forming truncated protein C123 of Streptococcus mutans (S. mutans), studied their biological functions in microbial proliferation and biofilm formation, and further investigated the underlying mechanism. Fourteen hexapeptides were simulated, 13 of which were successfully synthesized. We found that the amyloid-forming hexapeptides (AFhPs) displayed efficient broad-spectrum antibiofilm activity against the Gram-positive bacteria S. mutans, Streptococcus sanguis and Staphylococcus aureus, Gram-negative bacteria Escherichia coli and fungus Candida albicans, by aggregating into rigid amyloid fibres agglutinating microbes, whereas the non-amyloid-forming hexapeptides (non-AFhPs) did not. The AFhPs did not kill microbes and showed little or no cytotoxicity. Furthermore, a set of AFhPs displayed broad-spectrum antibiofilm activity, regardless of its source. The microbial cell wall carbohydrates, peptidoglycan (PGN), lipoteichoic acid (LTA), glucan and zymosan A, mediated AFhP binding and triggered significant AFhP fibrillation. Although amyloid fibres agglutinated lipid membrane model - large unilamellar vesicles (LUVs) - and LUVs facilitated AFhP fibrillation, the roles of lipid membranes in AFhP antibiofilm activities remain to be elucidated. We highlight the potential use of AFhPs as novel antibiofilm agents.
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