Mirror images of antimicrobial peptides provide reflections on their functions and amyloidogenic properties

Wang, Conan K., King, Gordon J., Conibear, Anne C., Ramos, Mariana C., Chaousis, Stephanie, Henriques, Sonia Troeira and Craik, David J. (2016) Mirror images of antimicrobial peptides provide reflections on their functions and amyloidogenic properties. Journal of American Chemical Society, 138 17: 5706-5713. doi:10.1021/jacs.6b02575


Author Wang, Conan K.
King, Gordon J.
Conibear, Anne C.
Ramos, Mariana C.
Chaousis, Stephanie
Henriques, Sonia Troeira
Craik, David J.
Title Mirror images of antimicrobial peptides provide reflections on their functions and amyloidogenic properties
Journal name Journal of American Chemical Society   Check publisher's open access policy
ISSN 0002-7863
1943-2984
1520-5126
Publication date 2016-04-11
Year available 2016
Sub-type Article (original research)
DOI 10.1021/jacs.6b02575
Open Access Status Not Open Access
Volume 138
Issue 17
Start page 5706
End page 5713
Total pages 8
Place of publication Washington, DC United States
Publisher American Chemical Society
Collection year 2017
Language eng
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.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: HERDC Pre-Audit
Institute for Molecular Bioscience - Publications
 
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Created: Tue, 17 May 2016, 01:45:20 EST by Susan Allen on behalf of Institute for Molecular Bioscience