Significance The formation of cross-α amyloids has been shown by crystallographic analysis of the highly cytolytic peptide PSMα3, a secreted virulence factor associated with the human pathogen Staphylococcus aureus . However, the relationship of the crystallographic cross-α structure to self-assembled filaments of PSMα3 and its relevance to other phenol-soluble modulin (PSM) peptides remained an open question. We report the cryo–electron microscopy structural analysis of three nanotubes derived from self-assembly of PSMα3 and PSMβ2 peptides in aqueous solution. In each case, the nanotubes are derived from self-association of cross-α amyloid protofilaments. The self-assembly behavior of S. aureus PSMα3 and PSMβ2 peptides provides strong evidence for the importance of the cross-α fold in self-assembled peptide and protein structures in general and for PSMs in particular.
Peptides In Aqueous Solution Phenol-soluble Modulin Self-assembled Peptide Formation Of Amyloids Protein Structures Self-assembled Protein Aqueous Solution Relationship Of Structure Self-assembled Structures Peptide Structures
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Round-ups are the summaries of handpicked papers around trending topics published every week. These would enable you to scan through a collection of papers and decide if the paper is relevant to you before actually investing time into reading it.
Climate change Research Articles published between Nov 14, 2022 to Nov 20, 2022
Nov 21, 2022
Articles Included: 2
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