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10.1002/cmdc.201700694 http://scihub22266oqcxt.onion/10.1002/cmdc.201700694 C5900894!5900894 !29265636     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=29265636 &cmd=llinks): Failed to open stream: HTTP request failed! 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Co-administration of Antimicrobial Peptides Enhances Toll-like Receptor?4 Antagonist Activity of a Synthetic Glycolipid |pdf=|usr=}}{{29265636 }} gab.com Text Co-administration of Antimicrobial Peptides Enhances Toll-like Receptor 4 Antagonist Activity of a Synthetic Glycolipid JO: ChemMedChem http://www.kidney.de/pget.php?&tw=1&pmid=29265636 #FOAvip This study examines the effect of co-administration of antimicrobial peptides and the synthetic glycolipid FP7, which is active in inhibiting inflammatory cytokine production caused by TLR4 activation and signaling. The co-administration of two lipopolysaccharide (LPS)-neutralizing peptides (a cecropin?A-melittin hybrid peptide and a human cathelicidin) enhances by an order of magnitude the potency of FP7 in blocking the TLR4 signal. Interestingly, this is not an additional effect of LPS neutralization by peptides, because it also occurs if cells are stimulated by the plant lectin phytohemagglutinin, a non-LPS TLR4 agonist. Our data suggest a dual mechanism of action for the peptides, not exclusively based on LPS binding and neutralization, but also on a direct effect on the LPS-binding proteins of the TLR4 receptor complex. NMR experiments in solution show that peptide addition changes the aggregation state of FP7, promoting the formation of larger micelles. These results suggest a relationship between the aggregation state of lipid?A-like ligands and the type and intensity of the TLR4 response. Twit Text FOAVip Co-administration of Antimicrobial Peptides Enhances Toll-like Receptor 4 Antagonist Activity of a Synthetic Glycolipid ????ChemMedChem http://www.kidney.de/pget.php?&tw=1&pmid=29265636 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29265636 #FOAvip English Wikipedia <ref>{{Cite pmid|29265636 }}</ref> Co-administration of Antimicrobial Peptides Enhances Toll-like Receptor?4 Antagonist Activity of a Synthetic Glycolipid #MMPMID29265636 Facchini FA ; Coelho H ; Sestito SE ; Delgado S ; Minotti A ; Andreu D ; Jiménez-Barbero J ; Peri F ChemMedChem 2018[Feb]; 13 (3 ): 280-287 PMID29265636 show ga This study examines the effect of co-administration of antimicrobial peptides and the synthetic glycolipid FP7, which is active in inhibiting inflammatory cytokine production caused by TLR4 activation and signaling. The co-administration of two lipopolysaccharide (LPS)-neutralizing peptides (a cecropin?A-melittin hybrid peptide and a human cathelicidin) enhances by an order of magnitude the potency of FP7 in blocking the TLR4 signal. Interestingly, this is not an additional effect of LPS neutralization by peptides, because it also occurs if cells are stimulated by the plant lectin phytohemagglutinin, a non-LPS TLR4 agonist. Our data suggest a dual mechanism of action for the peptides, not exclusively based on LPS binding and neutralization, but also on a direct effect on the LPS-binding proteins of the TLR4 receptor complex. NMR experiments in solution show that peptide addition changes the aggregation state of FP7, promoting the formation of larger micelles. These results suggest a relationship between the aggregation state of lipid?A-like ligands and the type and intensity of the TLR4 response. |Acute-Phase Proteins/metabolism [MESH] |Antimicrobial Cationic Peptides/*chemistry/pharmacology [MESH] |Carrier Proteins/metabolism [MESH] |Cathelicidins [MESH] |Cell Line [MESH] |Cell Survival/drug effects [MESH] |Glycolipids/*chemistry/pharmacology [MESH] |Humans [MESH] |Ligands [MESH] |Melitten/*chemistry/pharmacology [MESH] |Membrane Glycoproteins/metabolism [MESH] |Protein Binding [MESH] |Protein Conformation [MESH]Co-administration of Antimicrobial Peptides Enhances Toll-like Recepto(epmc).pdf DeepDyve Pubget Overpricing