Lipid head group discrimination by antimicrobial peptide LL-37: Insight into mechanism of action. Export

@article{citeulike:406767, abstract = {Abstract Interaction of the human antimicrobial peptide LL-37 with lipid monolayers has been investigated by a range of complementary techniques including pressure-area isotherms, insertion assay, epifluorescence microscopy, and synchrotron X-ray scattering, in order to analyze its mechanism of action. Lipid monolayers were formed at the air-liquid interface to mimic the surface of the bacterial cell wall and the outer leaflet of erythrocyte cell membrane by using phosphatidylglycerol, phosphatidylcholine and phosphatidylethanolamine lipids. LL-37 is found to readily insert into phosphatidylglycerol (DPPG) monolayers, disrupting their structure and thus indicating bactericidal action. In contrast, DPPC and DPPE monolayers remained virtually unaffected by LL-37, demonstrating its non-hemolytic activity and lipid discrimination. Specular X-ray reflectivity (XR) data yielded considerable differences in layer thickness and electron density profile after addition of the peptide to DPPG monolayer, but little change was seen after peptide injection when probing monolayers composed of DPPC and DPPE. Grazing incidence X-ray diffraction (GIXD) demonstrated significant peptide insertion and lateral packing order disruption of the DPPG monolayer by LL-37 insertion. Epifluorescence microscopy data support these findings.}, address = {University of Leeds.}, author = {Neville, Frances and Cahuzac, Marjolaine and Konovalov, Oleg and Ishitsuka, Yuji and Lee, Ka Yee C Y. and Kuzmenko, Ivan and Kale, Girish and Gidalevitz, David}, citeulike-article-id = {406767}, citeulike-linkout-0 = {http://dx.doi.org/10.1529/biophysj.105.067595}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/16299073}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=16299073}, day = {18}, doi = {10.1529/biophysj.105.067595}, issn = {0006-3495}, journal = {Biophys J}, keywords = {antimicrobial, biophysics, peptide}, month = {November}, posted-at = {2005-11-24 01:59:56}, priority = {3}, title = {Lipid head group discrimination by antimicrobial peptide LL-37: Insight into mechanism of action.}, url = {http://dx.doi.org/10.1529/biophysj.105.067595}, year = {2005} }

TY - JOUR ID - citeulike:406767 L3 - citeulike-article-id:406767 N2 - Abstract Interaction of the human antimicrobial peptide LL-37 with lipid monolayers has been investigated by a range of complementary techniques including pressure-area isotherms, insertion assay, epifluorescence microscopy, and synchrotron X-ray scattering, in order to analyze its mechanism of action. Lipid monolayers were formed at the air-liquid interface to mimic the surface of the bacterial cell wall and the outer leaflet of erythrocyte cell membrane by using phosphatidylglycerol, phosphatidylcholine and phosphatidylethanolamine lipids. LL-37 is found to readily insert into phosphatidylglycerol (DPPG) monolayers, disrupting their structure and thus indicating bactericidal action. In contrast, DPPC and DPPE monolayers remained virtually unaffected by LL-37, demonstrating its non-hemolytic activity and lipid discrimination. Specular X-ray reflectivity (XR) data yielded considerable differences in layer thickness and electron density profile after addition of the peptide to DPPG monolayer, but little change was seen after peptide injection when probing monolayers composed of DPPC and DPPE. Grazing incidence X-ray diffraction (GIXD) demonstrated significant peptide insertion and lateral packing order disruption of the DPPG monolayer by LL-37 insertion. Epifluorescence microscopy data support these findings. JF - Biophys J SN - 0006-3495 AD - University of Leeds. TI - Lipid head group discrimination by antimicrobial peptide LL-37: Insight into mechanism of action. KW - antimicrobial KW - biophysics KW - peptide AU - Neville, Frances AU - Cahuzac, Marjolaine AU - Konovalov, Oleg AU - Ishitsuka, Yuji AU - Lee, Ka Yee C AU - Kuzmenko, Ivan AU - Kale, Girish AU - Gidalevitz, David PY - 2005/11/18/ UR - http://dx.doi.org/10.1529/biophysj.105.067595 ER -