AI Article Synopsis
- - Enantiomers of BTD-2, PG-1, and PM-1 were created to study the structure and action of specific antimicrobial peptides that interact with membranes without needing receptors.
- - The crystal structure of BTD-2, determined to a high resolution, reveals a unique antiparallel trimer formation that may contribute to its effectiveness in disrupting membrane integrity.
- - This trimeric structure of BTD-2 extends into a larger supramolecular arrangement similar to amyloid fibrils, indicating a novel assembly pattern for antimicrobial peptides that connects their functions to those of amyloid-forming peptides.
Article Abstract
Enantiomeric forms of BTD-2, PG-1, and PM-1 were synthesized to delineate the structure and function of these β-sheet antimicrobial peptides. Activity and lipid-binding assays confirm that these peptides act via a receptor-independent mechanism involving membrane interaction. The racemic crystal structure of BTD-2 solved at 1.45 Å revealed a novel oligomeric form of β-sheet antimicrobial peptides within the unit cell: an antiparallel trimer, which we suggest might be related to its membrane-active form. The BTD-2 oligomer extends into a larger supramolecular state that spans the crystal lattice, featuring a steric-zipper motif that is common in structures of amyloid-forming peptides. The supramolecular structure of BTD-2 thus represents a new mode of fibril-like assembly not previously observed for antimicrobial peptides, providing structural evidence linking antimicrobial and amyloid peptides.
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| http://dx.doi.org/10.1021/jacs.6b02575 | DOI Listing |
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