Structure of Chemokine-Derived Antimicrobial Peptide Interleukin-8α and Interaction with Detergent Micelles and Oriented Lipid Bilayers Export

@article{citeulike:6061330, abstract = {PMID: 19813761 Interleukin-8α (IL-8α) is an antimicrobial peptide derived from the chemokine IL-8. Solution NMR was used to determine the atomic-resolution structure of IL-8α in SDS micelles. Solid-state NMR and tryptophan fluorescence were used to probe the interaction of IL-8α 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 2H 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-8α 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. 15N solid-state NMR spectra indicated a similar, nearly parallel position for the peptide in POPC/POPG bilayers. 31P and 2H 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.}, author = {Bourbigot, Sarah and Fardy, Liam and Waring, Alan J. and Yeaman, Michael R. and Booth, Valerie}, citeulike-article-id = {6061330}, citeulike-linkout-0 = {http://dx.doi.org/10.1021/bi901311p}, citeulike-linkout-1 = {http://pubs.acs.org/doi/abs/10.1021/bi901311p}, day = {10}, doi = {10.1021/bi901311p}, journal = {Biochemistry}, keywords = {antimicrobial-peptide}, month = {November}, number = {44}, pages = {10509--10521}, posted-at = {2009-11-03 19:12:09}, priority = {2}, title = {Structure of Chemokine-Derived Antimicrobial Peptide Interleukin-8α and Interaction with Detergent Micelles and Oriented Lipid Bilayers}, url = {http://dx.doi.org/10.1021/bi901311p}, volume = {48}, year = {2009} }

TY - JOUR ID - citeulike:6061330 L3 - citeulike-article-id:6061330 N2 - PMID: 19813761 Interleukin-8α (IL-8α) is an antimicrobial peptide derived from the chemokine IL-8. Solution NMR was used to determine the atomic-resolution structure of IL-8α in SDS micelles. Solid-state NMR and tryptophan fluorescence were used to probe the interaction of IL-8α 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 2H 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-8α 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. 15N solid-state NMR spectra indicated a similar, nearly parallel position for the peptide in POPC/POPG bilayers. 31P and 2H 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. IS - 44 JF - Biochemistry EP - 10521 TI - Structure of Chemokine-Derived Antimicrobial Peptide Interleukin-8α and Interaction with Detergent Micelles and Oriented Lipid Bilayers VL - 48 SP - 10509 KW - antimicrobial-peptide AU - Bourbigot, Sarah AU - Fardy, Liam AU - Waring, Alan AU - Yeaman, Michael AU - Booth, Valerie PY - 2009/11/10/ UR - http://dx.doi.org/10.1021/bi901311p ER -