Structural highlights
Publication Abstract from PubMed
Enantiomeric forms of BTD-2, PG-1, and PM-1 were synthesized to delineate the structure and function of these beta-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 A revealed a novel oligomeric form of beta-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.
Mirror Images of Antimicrobial Peptides Provide Reflections on Their Functions and Amyloidogenic Properties.,Wang CK, King GJ, Conibear AC, Ramos MC, Chaousis S, Henriques ST, Craik DJ J Am Chem Soc. 2016 May 4;138(17):5706-13. doi: 10.1021/jacs.6b02575. Epub 2016, Apr 26. PMID:27064294[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang CK, King GJ, Conibear AC, Ramos MC, Chaousis S, Henriques ST, Craik DJ. Mirror Images of Antimicrobial Peptides Provide Reflections on Their Functions and Amyloidogenic Properties. J Am Chem Soc. 2016 May 4;138(17):5706-13. doi: 10.1021/jacs.6b02575. Epub 2016, Apr 26. PMID:27064294 doi:http://dx.doi.org/10.1021/jacs.6b02575
