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10.1038/s41598-017-01474-0 http://scihub22266oqcxt.onion/10.1038/s41598-017-01474-0 C5431190!5431190 !28469145     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28469145 &cmd=llinks): Failed to open stream: HTTP request failed! 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Investigation of cationicity and structure of pseudin-2 analogues for enhanced bacterial selectivity and anti-inflammatory activity |pdf=|usr=}}{{28469145 }} gab.com Text Investigation of cationicity and structure of pseudin-2 analogues for enhanced bacterial selectivity and anti-inflammatory activity JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=28469145 #FOAvip Pseudin-2 (Ps), isolated from the frog Pseudis paradoxa, exhibits potent antibacterial activity and cytotoxicity. To develop antimicrobial peptides with anti-inflammatory activity and low cytotoxicity, we designed Ps analogues with Lys substitutions, resulting in elevated amphipathic ?-helical structure and cationicity. We further substituted Gly(11) with Pro (Ps-P analogues) to increase bacterial cell selectivity. Ps analogues retained antimicrobial activity and exhibited reduced cytotoxicity, whereas Ps-P analogues exhibited lower cytotoxicity and antimicrobial activity. Tertiary structures revealed that Ps has a linear ?-helix from Leu(2) to Glu(24), whereas Ps-P has a bend at Pro(11) between two short ?-helixes. Using various biophysical experiments, we found that Ps analogues produced much higher membrane depolarization than Ps-P analogues, whereas Ps-P analogues may penetrate bacterial cell membranes. Ps and its analogue Ps-K18 exhibited potent anti-inflammatory activity in LPS-stimulated RAW264.7 and mouse dendritic cells via a mechanism involving the Toll-like receptor 4 (TLR4) pathway. These activities may arise from their direct inhibition of the formation of TLR4-MD-2_LPS complex, implying that amphipathic ?-helical structure with an optimum balance between enhanced cationicity and hydrophobicity may be essential for their anti-inflammatory activity. The bent structure provided by Pro substitution plays an important role in enhancing bacterial cell selectivity and cell penetration. Twit Text FOAVip Investigation of cationicity and structure of pseudin-2 analogues for enhanced bacterial selectivity and anti-inflammatory activity ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=28469145 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28469145 #FOAvip English Wikipedia <ref>{{Cite pmid|28469145 }}</ref> Investigation of cationicity and structure of pseudin-2 analogues for enhanced bacterial selectivity and anti-inflammatory activity #MMPMID28469145 Jeon D ; Jeong MC ; Jacob B ; Bang JK ; Kim EH ; Cheong C ; Jung ID ; Park Y ; Kim Y Sci Rep 2017[May]; 7 (1 ): 1455 PMID28469145 show ga Pseudin-2 (Ps), isolated from the frog Pseudis paradoxa, exhibits potent antibacterial activity and cytotoxicity. To develop antimicrobial peptides with anti-inflammatory activity and low cytotoxicity, we designed Ps analogues with Lys substitutions, resulting in elevated amphipathic ?-helical structure and cationicity. We further substituted Gly(11) with Pro (Ps-P analogues) to increase bacterial cell selectivity. Ps analogues retained antimicrobial activity and exhibited reduced cytotoxicity, whereas Ps-P analogues exhibited lower cytotoxicity and antimicrobial activity. Tertiary structures revealed that Ps has a linear ?-helix from Leu(2) to Glu(24), whereas Ps-P has a bend at Pro(11) between two short ?-helixes. Using various biophysical experiments, we found that Ps analogues produced much higher membrane depolarization than Ps-P analogues, whereas Ps-P analogues may penetrate bacterial cell membranes. Ps and its analogue Ps-K18 exhibited potent anti-inflammatory activity in LPS-stimulated RAW264.7 and mouse dendritic cells via a mechanism involving the Toll-like receptor 4 (TLR4) pathway. These activities may arise from their direct inhibition of the formation of TLR4-MD-2_LPS complex, implying that amphipathic ?-helical structure with an optimum balance between enhanced cationicity and hydrophobicity may be essential for their anti-inflammatory activity. The bent structure provided by Pro substitution plays an important role in enhancing bacterial cell selectivity and cell penetration. |Amino Acid Sequence [MESH] |Amino Acid Substitution [MESH] |Amphibian Proteins/chemical synthesis/*chemistry/pharmacology [MESH] |Animals [MESH] |Anti-Bacterial Agents/chemical synthesis/*chemistry/pharmacology [MESH] |Antimicrobial Cationic Peptides/chemical synthesis/*chemistry/pharmacology [MESH] |Anura [MESH] |Dendritic Cells/cytology/drug effects/immunology [MESH] |Female [MESH] |Gene Expression Regulation [MESH] |Gram-Negative Bacteria/drug effects/growth & development [MESH] |Gram-Positive Bacteria/drug effects/growth & development [MESH] |Humans [MESH] |Lipopolysaccharides/pharmacology [MESH] |Lymphocyte Antigen 96/genetics/immunology [MESH] |Lysine/*chemistry [MESH] |Mice [MESH] |Mice, Inbred C57BL [MESH] |Microbial Sensitivity Tests [MESH] |Primary Cell Culture [MESH] |Proline/*chemistry [MESH] |Protein Engineering [MESH] |Protein Structure, Tertiary [MESH] |RAW 264.7 Cells [MESH] |Solid-Phase Synthesis Techniques [MESH]Investigation of cationicity and structure of pseudin-2 analogues for (epmc).pdf DeepDyve Pubget Overpricing