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10.1021/acs.molpharmaceut.5b00177 http://scihub22266oqcxt.onion/10.1021/acs.molpharmaceut.5b00177 C4533831!4533831!25955351     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Mol+Pharm 2015 ; 12 (6): 2180-8 Nephropedia Template TP {{tp|p=25955351|t=2015. Discovery of Peptide Ligands for Hepatic Stellate Cells Using Phage Display |pdf=|usr=}}{{25955351}} gab.com Text Discovery of Peptide Ligands for Hepatic Stellate Cells Using Phage Display JO: Mol Pharm http://www.kidney.de/pget.php?&tw=1&pmid=25955351 #FOAvip Regardless of its cause, liver fibrosis is characterized by the excessive accumulation of extracellular matrix (ECM) in the liver. Hepatic stellate cells (HSCs) are the main producers responsible for the excessive production of ECM and profibrogenic cytokines in fibrotic liver. Therefore, development of HSC-specific delivery systems is essential for the success of antifibrotic agents. The objective of this study is to identify peptide ligands targeting the insulin like growth factor 2 receptor (IGF2R), which is overexpressed on HSCs. We expect to use the peptide ligands for the future development of HSC-targeted drug delivery system.Protein- and whole cell-based phage display biopannings were conducted to identify phage/peptide candidates. Phage ELISA, cellular uptake and cell viability assay were employed to evaluate the binding affinity and specificity of these peptide ligands to recombinant human IGF2R and HSCs. IGF2R siRNA was used to silence the IGF2R protein expression in human hepatic stellate cells (LX-2) to confirm the specificity of the identified peptide ligands.Among the identified peptide candidates, the peptide-431 shows the highest binding affinity and specificity to recombinant human IGF2R protein and HSCs. The equilibrium dissociation constant (Kd) of the peptide-431 is 6.19 ?M for LX-2 cells and 12.35 ?M for rat hepatic stellate cells HSC-T6. Cellular uptake of the peptide-431 in LX-2 cells is significantly reduced after silencing IGF2R with siRNA. The peptide-431 also enhances the uptake of a proapoptotic peptide (KLA peptide) in LX-2 and HSC-T6 cells, indicating that the peptide-431 can be used as a targeting ligand to deliver antifibrotic agents into not only rat but also human HSCs. Dimerization of the peptide-431 further increase its binding affinity to LX-2 cells by approximately nine-fold. Twit Text FOAVip Discovery of Peptide Ligands for Hepatic Stellate Cells Using Phage Display ????Mol Pharm http://www.kidney.de/pget.php?&tw=1&pmid=25955351 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25955351 #FOAvip English Wikipedia <ref>{{Cite pmid|25955351}}</ref> Discovery of Peptide Ligands for Hepatic Stellate Cells Using Phage Display #MMPMID25955351 Chen Z; Jin W; Liu H; Zhao Z; Cheng K Mol Pharm 2015[Jun]; 12 (6): 2180-8 PMID25955351show ga Regardless of its cause, liver fibrosis is characterized by the excessive accumulation of extracellular matrix (ECM) in the liver. Hepatic stellate cells (HSCs) are the main producers responsible for the excessive production of ECM and profibrogenic cytokines in fibrotic liver. Therefore, development of HSC-specific delivery systems is essential for the success of antifibrotic agents. The objective of this study is to identify peptide ligands targeting the insulin like growth factor 2 receptor (IGF2R), which is overexpressed on HSCs. We expect to use the peptide ligands for the future development of HSC-targeted drug delivery system.Protein- and whole cell-based phage display biopannings were conducted to identify phage/peptide candidates. Phage ELISA, cellular uptake and cell viability assay were employed to evaluate the binding affinity and specificity of these peptide ligands to recombinant human IGF2R and HSCs. IGF2R siRNA was used to silence the IGF2R protein expression in human hepatic stellate cells (LX-2) to confirm the specificity of the identified peptide ligands.Among the identified peptide candidates, the peptide-431 shows the highest binding affinity and specificity to recombinant human IGF2R protein and HSCs. The equilibrium dissociation constant (Kd) of the peptide-431 is 6.19 ?M for LX-2 cells and 12.35 ?M for rat hepatic stellate cells HSC-T6. Cellular uptake of the peptide-431 in LX-2 cells is significantly reduced after silencing IGF2R with siRNA. The peptide-431 also enhances the uptake of a proapoptotic peptide (KLA peptide) in LX-2 and HSC-T6 cells, indicating that the peptide-431 can be used as a targeting ligand to deliver antifibrotic agents into not only rat but also human HSCs. Dimerization of the peptide-431 further increase its binding affinity to LX-2 cells by approximately nine-fold. äDiscovery of Peptide Ligands for Hepatic Stellate Cells Using Phage Di(epmc).pdf DeepDyve Pubget Overpricing