Mirror Images of Antimicrobial Peptides Provide Reflections on Their Functions and Amyloidogenic Properties
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- 作者：Conan K. Wang ; Gordon J. King ; Anne C. Conibear ; Mariana C. Ramos ; Stephanie Chaousis ; Sónia Troeira Henriques ; David J. Craik
- 刊名：Journal of the American Chemical Society
- 出版年：2016
- 出版时间：May 4, 2016
- 年：2016
- 卷：138
- 期：17
- 页码：5706-5713
- 全文大小：601K
- 年卷期：0
- ISSN：1520-5126
文摘
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.