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10.1021/cb500475y http://scihub22266oqcxt.onion/10.1021/cb500475y C4168778!4168778!25061850     free     free     free Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       ACS+Chem+Biol 2014 ; 9 (9): 1997-2002 Nephropedia Template TP {{tp|p=25061850|t=2014. Transformation of Human Cathelicidin LL-37 into Selective, Stable, and Potent Antimicrobial Compounds |pdf=|usr=}}{{25061850}} gab.com Text Transformation of Human Cathelicidin LL-37 into Selective, Stable, and Potent Antimicrobial Compounds JO: ACS Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=25061850 #FOAvip This Letter reports a family of novel antimicrobial compounds obtained by combining peptide library screening with structure-based design. Library screening led to the identification of a human LL-37 peptide resistant to chymotrypsin. This d-amino-acid-containing peptide template was active against Escherichia coli but not methicillin-resistant Staphylococcus aureus (MRSA). It possesses a unique nonclassic amphipathic structure with hydrophobic defects. By repairing the hydrophobic defects, the peptide (17BIPHE2) gained activity against the ESKAPE pathogens, including Enterococcus faecium, S. aureus, Klebsiella pneumoniae, Acinetobacter baumanii, Pseudomonas aeruginosa, and Enterobacter species. In vitro, 17BIPHE2 could disrupt bacterial membranes and bind to DNA. In vivo, the peptide prevented staphylococcal biofilm formation in a mouse model of catheter-associated infection. Meanwhile, it boosted the innate immune response to further combat the infection. Because these peptides are potent, cell-selective, and stable to several proteases, they may be utilized to combat one or more ESKAPE pathogens. Twit Text FOAVip Transformation of Human Cathelicidin LL-37 into Selective, Stable, and Potent Antimicrobial Compounds ????ACS Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=25061850 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25061850 #FOAvip English Wikipedia <ref>{{Cite pmid|25061850}}</ref> Transformation of Human Cathelicidin LL-37 into Selective, Stable, and Potent Antimicrobial Compounds #MMPMID25061850 Wang G; Hanke ML; Mishra B; Lushnikova T; Heim C; Chittezham Thomas V; Bayles KW; Kielian T ACS Chem Biol 2014[Sep]; 9 (9): 1997-2002 PMID25061850show ga This Letter reports a family of novel antimicrobial compounds obtained by combining peptide library screening with structure-based design. Library screening led to the identification of a human LL-37 peptide resistant to chymotrypsin. This d-amino-acid-containing peptide template was active against Escherichia coli but not methicillin-resistant Staphylococcus aureus (MRSA). It possesses a unique nonclassic amphipathic structure with hydrophobic defects. By repairing the hydrophobic defects, the peptide (17BIPHE2) gained activity against the ESKAPE pathogens, including Enterococcus faecium, S. aureus, Klebsiella pneumoniae, Acinetobacter baumanii, Pseudomonas aeruginosa, and Enterobacter species. In vitro, 17BIPHE2 could disrupt bacterial membranes and bind to DNA. In vivo, the peptide prevented staphylococcal biofilm formation in a mouse model of catheter-associated infection. Meanwhile, it boosted the innate immune response to further combat the infection. Because these peptides are potent, cell-selective, and stable to several proteases, they may be utilized to combat one or more ESKAPE pathogens. äTransformation of Human Cathelicidin LL-37 into Selective, Stable, and(epmc).pdf DeepDyve Pubget Overpricing