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Structure of Chemokine-Derived Antimicrobial Peptide Interleukin-8α and Interaction with Detergent Micelles and Oriented Lipid Bilayers
- Source :
- Biochemistry. 48:10509-10521
- Publication Year :
- 2009
- Publisher :
- American Chemical Society (ACS), 2009.
-
Abstract
- Interleukin-8alpha (IL-8alpha) is an antimicrobial peptide derived from the chemokine IL-8. Solution NMR was used to determine the atomic-resolution structure of IL-8alpha in SDS micelles. Solid-state NMR and tryptophan fluorescence were used to probe the interaction of IL-8alpha with model membranes. The peptide interacted differently with anionic versus purely zwitterionic micelles or bilayers. Tryptophan fluorescence demonstrated a deeper position of Trp4 in SDS micelles and POPC/POPG bilayers compared to pure POPC bilayers, consistent with (2)H order parameters, which also indicated a deeper position of the peptide in POPC/POPG bilayers compared to POPC bilayers. Paramagnetic probe data showed that IL-8alpha was situated roughly parallel to the SDS micelle surface, with a slight tilt that positioned the N-terminus more deeply in the micelle compared to the C-terminus. (15)N solid-state NMR spectra indicated a similar, nearly parallel position for the peptide in POPC/POPG bilayers. (31)P and (2)H solid-state NMR demonstrated that the peptide did not induce the formation of any nonlamellar phases and did not significantly disrupt bilayer orientation in aligned model membranes composed of POPC or POPC and POPG.
- Subjects :
- Models, Molecular
Circular dichroism
Detergents
Lipid Bilayers
Molecular Sequence Data
Peptide
Biochemistry
Micelle
Article
chemistry.chemical_compound
Amino Acid Sequence
Sodium dodecyl sulfate
Lipid bilayer
Nuclear Magnetic Resonance, Biomolecular
POPC
Micelles
chemistry.chemical_classification
Chromatography
Circular Dichroism
Interleukin-8
technology, industry, and agriculture
Sodium Dodecyl Sulfate
NMR spectra database
Crystallography
Spectrometry, Fluorescence
Membrane
chemistry
lipids (amino acids, peptides, and proteins)
Subjects
Details
- ISSN :
- 15204995 and 00062960
- Volume :
- 48
- Database :
- OpenAIRE
- Journal :
- Biochemistry
- Accession number :
- edsair.doi.dedup.....7c1d34860e18a56cdfc57648d618beb6