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10.1007/s00249-016-1180-8 http://scihub22266oqcxt.onion/10.1007/s00249-016-1180-8 C5384954!5384954 !27832293     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\27832293 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Eur+Biophys+J 2017 ; 46 (4 ): 375-382 Nephropedia Template TP {{tp|p=27832293 |t=2017. Modulating charge-dependent and folding-mediated antimicrobial interactions at peptide-lipid interfaces |pdf=|usr=}}{{27832293 }} gab.com Text Modulating charge-dependent and folding-mediated antimicrobial interactions at peptide-lipid interfaces JO: Eur Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=27832293 #FOAvip Peptide-lipid interactions support a variety of biological functions. Of particular interest are those that underpin fundamental mechanisms of innate immunity that are programmed in host defense or antimicrobial peptide sequences found virtually in all multicellular organisms. Here we synthetically modulate antimicrobial peptide-lipid interactions using an archetypal helical antimicrobial peptide and synthetic membranes mimicking bacterial and mammalian membranes in solution. We probe these interactions as a function of membrane-induced folding, membrane stability and peptide-lipid ratios using a correlative approach encompassing light scattering and spectroscopy measurements such as circular dichroism spectroscopy, fluorescence and nuclear magnetic resonance spectroscopy. The peptide behavior is assessed against that of its anionic counterpart having similar propensities for ?-helical folding. The results indicate strong correlations between peptide folding and membrane type, supporting folding-responsive binding of antimicrobial peptides to bacterial membranes. The study provides a straightforward approach for modulating structure-activity relationships in the context of membrane-induced antimicrobial action, thus holding promise for the rational design of potent antimicrobial agents. Twit Text FOAVip Modulating charge-dependent and folding-mediated antimicrobial interactions at peptide-lipid interfaces ????Eur Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=27832293 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27832293 #FOAvip English Wikipedia <ref>{{Cite pmid|27832293 }}</ref> Modulating charge-dependent and folding-mediated antimicrobial interactions at peptide-lipid interfaces #MMPMID27832293 Iavicoli P ; Rossi F ; Lamarre B ; Bella A ; Ryadnov MG ; Calzolai L Eur Biophys J 2017[May]; 46 (4 ): 375-382 PMID27832293 show ga Peptide-lipid interactions support a variety of biological functions. Of particular interest are those that underpin fundamental mechanisms of innate immunity that are programmed in host defense or antimicrobial peptide sequences found virtually in all multicellular organisms. Here we synthetically modulate antimicrobial peptide-lipid interactions using an archetypal helical antimicrobial peptide and synthetic membranes mimicking bacterial and mammalian membranes in solution. We probe these interactions as a function of membrane-induced folding, membrane stability and peptide-lipid ratios using a correlative approach encompassing light scattering and spectroscopy measurements such as circular dichroism spectroscopy, fluorescence and nuclear magnetic resonance spectroscopy. The peptide behavior is assessed against that of its anionic counterpart having similar propensities for ?-helical folding. The results indicate strong correlations between peptide folding and membrane type, supporting folding-responsive binding of antimicrobial peptides to bacterial membranes. The study provides a straightforward approach for modulating structure-activity relationships in the context of membrane-induced antimicrobial action, thus holding promise for the rational design of potent antimicrobial agents. |*Protein Folding [MESH] |Amino Acid Sequence [MESH] |Antimicrobial Cationic Peptides/*chemistry/*metabolism [MESH] |Cell Membrane/metabolism [MESH] |Protein Binding [MESH]Modulating charge-dependent and folding-mediated antimicrobial interac(epmc).pdf DeepDyve Pubget Overpricing