De Novo Designed α-Sheet Peptides Inhibit Functional Amyloid Formation of Streptococcus mutans Biofilms

Journal of Molecular Biology
Natasha Paranjapye, Valerie Daggett

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 funct...Continue Reading

Citations

Oct 24, 2019·Interface Focus·E James Milner-White
Jul 28, 2020·Protein Science : a Publication of the Protein Society·Dennis Bromley, Valerie Daggett
Feb 13, 2020·International Journal of Molecular Sciences·Anand BalupuriNam Sook Kang
Jun 15, 2021·Frontiers in Aging Neuroscience·Shaochang WuZongxin Ling
Oct 15, 2019·Biochemistry·Matthew Carter Childers, Valerie Daggett

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