29 research outputs found
Rapid Detection of Ricin in Serum Based on Cu-Chelated Magnetic Beads Using Mass Spectrometry
No full textA Comparison of the Effects of Amide and Acid Groups at the C-Terminus on the Collision-Induced Dissociation of Deprotonated Peptides
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Ion/Ion Reactions with “Onium” Reagents: An Approach for the Gas-phase Transfer of Organic Cations to Multiply-Charged Anions
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Characterizing Peptide Neutral Losses Induced by Negative Electron-Transfer Dissociation (NETD)
No full textEffect of a high-protein diet on maintenance of blood pressure levels achieved after initial weight loss: the DiOGenes randomized study
No full textStructural effects of the antimicrobial peptide maculatin 1.1 on supported lipid bilayers
Get PDFThe interactions of the antimicrobial peptide maculatin 1.1 (GLFGVLAKVAAHVVPAIAEHF-NH2) with model phospholipid membranes were studied by use of dual polarisation interferometry and neutron reflectometry and dimyristoylphosphatidylcholine (DMPC) and mixed DMPC–dimyristoylphosphatidylglycerol (DMPG)-supported lipid bilayers chosen to mimic eukaryotic and prokaryotic membranes, respectively. In DMPC bilayers concentration-dependent binding and increasing perturbation of bilayer order by maculatin were observed. By contrast, in mixed DMPC–DMPG bilayers, maculatin interacted more strongly and in a concentration-dependent manner with retention of bilayer lipid order and structure, consistent with pore formation. These results emphasise the importance of membrane charge in mediating antimicrobial peptide activity and emphasise the importance of using complementary methods of analysis in probing the mode of action of antimicrobial peptides
Nerve conduction during acute blood-flow restriction with and without low-intensity exercise Nerve conduction and blood-flow restriction
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