Pore Structure, Thinning Effect, and Lateral Diffusive Dynamics of Oriented Lipid Membranes Interacting with Antimicrobial Peptide Protegrin-1: 31P and 2H Solid-State NMR Study Export

@article{citeulike:3125152, abstract = {Abstract: Membrane pores that are induced in oriented membranes by an antimicrobial peptide (AMP), protegrin-1 (PG-1), are investigated by 31P and 2H solid state NMR spectroscopy. We incorporated a well-studied peptide, protegrin-1 (PG-1), a ²-sheet AMP, to investigate AMP-induced dynamic supramolecular lipid assemblies at different peptide concentrations and membrane compositions. Anisotropic NMR line shapes specifying toroidal pores and thinned membranes, which are formed in membrane bilayers by the binding of AMPs, have been analyzed for the first time. Theoretical NMR line shapes of lipids distributed on the surface of toroidal pores and thinned membranes reproduce reasonably well the line shape characteristics of our experimentally measured 31P and 2H solid-state NMR spectra of oriented lipids binding with PG-1. The lateral diffusions of lipids are also analyzed from the motionally averaged one- and two-dimensional 31P and 2H solid-state NMR spectra of oriented lipids that are binding with AMPs.}, address = {Department of Chemistry, Virginia Tech, Blacksburg, Virginia 24061}, author = {Wi, Sungsool and Kim, Chul}, citeulike-article-id = {3125152}, citeulike-linkout-0 = {http://dx.doi.org/10.1021/jp801825k}, citeulike-linkout-1 = {http://pubs.acs.org/doi/abs/10.1021/jp801825k}, day = {14}, doi = {10.1021/jp801825k}, journal = {J. Phys. Chem. B}, keywords = {diffusion, lateral, membrane, pore, thinning, wi08pd}, month = {August}, posted-at = {2008-08-15 01:21:25}, priority = {5}, title = {Pore Structure, Thinning Effect, and Lateral Diffusive Dynamics of Oriented Lipid Membranes Interacting with Antimicrobial Peptide Protegrin-1: 31P and 2H Solid-State NMR Study}, url = {http://dx.doi.org/10.1021/jp801825k}, year = {2008} }

TY - JOUR ID - citeulike:3125152 L3 - citeulike-article-id:3125152 N2 - Abstract: Membrane pores that are induced in oriented membranes by an antimicrobial peptide (AMP), protegrin-1 (PG-1), are investigated by 31P and 2H solid state NMR spectroscopy. We incorporated a well-studied peptide, protegrin-1 (PG-1), a ²-sheet AMP, to investigate AMP-induced dynamic supramolecular lipid assemblies at different peptide concentrations and membrane compositions. Anisotropic NMR line shapes specifying toroidal pores and thinned membranes, which are formed in membrane bilayers by the binding of AMPs, have been analyzed for the first time. Theoretical NMR line shapes of lipids distributed on the surface of toroidal pores and thinned membranes reproduce reasonably well the line shape characteristics of our experimentally measured 31P and 2H solid-state NMR spectra of oriented lipids binding with PG-1. The lateral diffusions of lipids are also analyzed from the motionally averaged one- and two-dimensional 31P and 2H solid-state NMR spectra of oriented lipids that are binding with AMPs. JF - J. Phys. Chem. B AD - Department of Chemistry, Virginia Tech, Blacksburg, Virginia 24061 TI - Pore Structure, Thinning Effect, and Lateral Diffusive Dynamics of Oriented Lipid Membranes Interacting with Antimicrobial Peptide Protegrin-1: 31P and 2H Solid-State NMR Study KW - diffusion KW - lateral KW - membrane KW - pore KW - thinning KW - wi08pd AU - Wi, Sungsool AU - Kim, Chul PY - 2008/08/14/ UR - http://dx.doi.org/10.1021/jp801825k ER -