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10.1371/journal.pone.0132446 http://scihub22266oqcxt.onion/10.1371/journal.pone.0132446 C4511006!4511006 !26196285     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26196285 &cmd=llinks): Failed to open stream: HTTP request failed! 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Peptide Inhibitor of Complement C1 (PIC1) Rapidly Inhibits Complement Activation after Intravascular Injection in Rats |pdf=|usr=}}{{26196285 }} gab.com Text Peptide Inhibitor of Complement C1 (PIC1) Rapidly Inhibits Complement Activation after Intravascular Injection in Rats JO: PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=26196285 #FOAvip The complement system has been increasingly recognized to play a pivotal role in a variety of inflammatory and autoimmune diseases. Consequently, therapeutic modulators of the classical, lectin and alternative pathways of the complement system are currently in pre-clinical and clinical development. Our laboratory has identified a peptide that specifically inhibits the classical and lectin pathways of complement and is referred to as Peptide Inhibitor of Complement C1 (PIC1). In this study, we determined that the lead PIC1 variant demonstrates a salt-dependent binding to C1q, the initiator molecule of the classical pathway. Additionally, this peptide bound to the lectin pathway initiator molecule MBL as well as the ficolins H, M and L, suggesting a common mechanism of PIC1 inhibitory activity occurs via binding to the collagen-like tails of these collectin molecules. We further analyzed the effect of arginine and glutamic acid residue substitution on the complement inhibitory activity of our lead derivative in a hemolytic assay and found that the original sequence demonstrated superior inhibitory activity. To improve upon the solubility of the lead derivative, a pegylated, water soluble variant was developed, structurally characterized and demonstrated to inhibit complement activation in mouse plasma, as well as rat, non-human primate and human serum in vitro. After intravenous injection in rats, the pegylated derivative inhibited complement activation in the blood by 90% after 30 seconds, demonstrating extremely rapid function. Additionally, no adverse toxicological effects were observed in limited testing. Together these results show that PIC1 rapidly inhibits classical complement activation in vitro and in vivo and is functional for a variety of animal species, suggesting its utility in animal models of classical complement-mediated diseases. Twit Text FOAVip Peptide Inhibitor of Complement C1 (PIC1) Rapidly Inhibits Complement Activation after Intravascular Injection in Rats ????PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=26196285 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26196285 #FOAvip English Wikipedia <ref>{{Cite pmid|26196285 }}</ref> Peptide Inhibitor of Complement C1 (PIC1) Rapidly Inhibits Complement Activation after Intravascular Injection in Rats #MMPMID26196285 Sharp JA ; Hair PS ; Pallera HK ; Kumar PS ; Mauriello CT ; Nyalwidhe JO ; Phelps CA ; Park D ; Thielens NM ; Pascal SM ; Chen W ; Duffy DM ; Lattanzio FA ; Cunnion KM ; Krishna NK PLoS One 2015[]; 10 (7 ): e0132446 PMID26196285 show ga The complement system has been increasingly recognized to play a pivotal role in a variety of inflammatory and autoimmune diseases. Consequently, therapeutic modulators of the classical, lectin and alternative pathways of the complement system are currently in pre-clinical and clinical development. Our laboratory has identified a peptide that specifically inhibits the classical and lectin pathways of complement and is referred to as Peptide Inhibitor of Complement C1 (PIC1). In this study, we determined that the lead PIC1 variant demonstrates a salt-dependent binding to C1q, the initiator molecule of the classical pathway. Additionally, this peptide bound to the lectin pathway initiator molecule MBL as well as the ficolins H, M and L, suggesting a common mechanism of PIC1 inhibitory activity occurs via binding to the collagen-like tails of these collectin molecules. We further analyzed the effect of arginine and glutamic acid residue substitution on the complement inhibitory activity of our lead derivative in a hemolytic assay and found that the original sequence demonstrated superior inhibitory activity. To improve upon the solubility of the lead derivative, a pegylated, water soluble variant was developed, structurally characterized and demonstrated to inhibit complement activation in mouse plasma, as well as rat, non-human primate and human serum in vitro. After intravenous injection in rats, the pegylated derivative inhibited complement activation in the blood by 90% after 30 seconds, demonstrating extremely rapid function. Additionally, no adverse toxicological effects were observed in limited testing. Together these results show that PIC1 rapidly inhibits classical complement activation in vitro and in vivo and is functional for a variety of animal species, suggesting its utility in animal models of classical complement-mediated diseases. |Amino Acid Sequence [MESH] |Animals [MESH] |Complement Activation/*drug effects [MESH] |Complement C1q/*immunology [MESH] |Ficolins [MESH] |Humans [MESH] |Injections [MESH] |Lectins/immunology [MESH] |Macaca fascicularis [MESH] |Male [MESH] |Mannose-Binding Lectin/immunology [MESH] |Mice [MESH] |Molecular Sequence Data [MESH] |Peptides/administration & dosage/blood/*chemistry/*pharmacology [MESH] |Rats [MESH] |Rats, Wistar [MESH]Peptide Inhibitor of Complement C1 (PIC1) Rapidly Inhibits Complement (epmc).pdf DeepDyve Pubget Overpricing