Mirror Images of Antimicrobial Peptides Provide Reflections on Their Functions and Amyloidogenic Properties
| Autor: | Anne C. Conibear, David J. Craik, Gordon J. King, Sónia Troeira Henriques, Conan K. Wang, Mariana C. Ramos, Stephanie Chaousis |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Amyloid Circular dichroism 060110 Receptors and Membrane Biology Protein Conformation Stereochemistry Antimicrobial peptides Supramolecular chemistry racemic crystal structure Trimer β-sheet antimicrobial peptides Crystallography X-Ray 010402 general chemistry Antiparallel (biochemistry) 01 natural sciences Biochemistry Catalysis 03 medical and health sciences Colloid and Surface Chemistry Protein structure Anti-Infective Agents 030401 Biologically Active Molecules 060502 Infectious Agents Chemistry Circular Dichroism General Chemistry Surface Plasmon Resonance Antimicrobial Combinatorial chemistry 0104 chemical sciences 030104 developmental biology 030406 Proteins and Peptides peptide-lipid interactions Enantiomer Peptides |
| Zdroj: | Journal of the American Chemical Society |
| ISSN: | 1520-5126 0002-7863 |
| DOI: | 10.1021/jacs.6b02575 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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