Structural requirements for antimicrobial versus chemoattractant activities for dermaseptin S9

Dermaseptin S9 (Drs S9), GLRSKIWLWVLLMIWQESNKFKKM, isolated from frog skin, does not resemble any of the cationic and amphipathic antimicrobial peptides identified to date, having a highly hydrophobic core sequence flanked at either side by cationic termini. Previous studies [Lequin O, Ladram A, Cha...

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Published in:The FEBS journal 2008-08, Vol.275 (16), p.4134-4151
Main Authors: Auvynet, Constance, El Amri, Chahrazade, Lacombe, Claire, Bruston, Francine, Bourdais, Julie, Nicolas, Pierre, Rosenstein, Yvonne
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amyloid - chemistry
Anti-Bacterial Agents - chemistry
Anti-Bacterial Agents - pharmacology
Antimicrobial Cationic Peptides - chemistry
Antimicrobial Cationic Peptides - pharmacology
antimicrobial peptide
Anura
Biochemistry
Chemical Sciences
Chemotactic Factors - chemistry
Chemotactic Factors - pharmacology
chemotaxis
Chemotaxis - drug effects
dermaseptin
frog skin
Frogs
infrared spectroscopy
Lipid Bilayers - chemistry
Molecular Sequence Data
Molecular structure
Organic chemistry
Peptides
Protein Structure, Secondary
Receptors, G-Protein-Coupled - metabolism
Water
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Summary:Dermaseptin S9 (Drs S9), GLRSKIWLWVLLMIWQESNKFKKM, isolated from frog skin, does not resemble any of the cationic and amphipathic antimicrobial peptides identified to date, having a highly hydrophobic core sequence flanked at either side by cationic termini. Previous studies [Lequin O, Ladram A, Chabbert A, Bruston F, Convert O, Vanhoye D, Chassaing G, Nicolas P & Amiche M (2006) Biochemistry45, 468-480] demonstrated that this peptide adopted a non-amphipathic α-helical conformation in trifluoroethanol/water mixtures, but was highly aggregated in aqueous solutions and in the presence of sodium dodecyl sulfate micelles. Circular dichroism, FTIR and attenuated total reflectance FTIR spectroscopies, combined with a surface plasmon resonance study, show that Drs S9 forms stable and ordered β-sheet aggregates in aqueous buffers or when bound to anionic or zwitterionic phospholipid vesicles. These structures slowly assembled into amyloid-like fibrils in aqueous environments via spherical intermediates, as revealed by electron microscopy and Congo red staining. Drs S9 induced the directional migration of neutrophils, T lymphocytes and monocytes. Interestingly, the antimicrobial and chemotactic activities of Drs S9 are modulated by its amyloid-like properties. Whereas spherical oligomers of Drs S9 exhibit antimicrobial activity, the soluble, weakly self-associated forms of Drs S9 act on human leukocytes to promote chemotaxis and/or immunological response activation in the same range of concentration as amyloidogenic peptides Aβ(1-42), the most fibrillogenic isoform of amyloid beta peptides, and the prion peptide PrP(106-126).
ISSN:1742-464X
1742-4658
DOI:10.1111/j.1742-4658.2008.06554.x