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10.1016/j.bbrep.2015.07.019 http://scihub22266oqcxt.onion/10.1016/j.bbrep.2015.07.019 C5668852!5668852!29124175     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biochem+Biophys+Rep 2015 ; 3 (ä): 123-33 Nephropedia Template TP {{tp|p=29124175|t=2015. Transthyretin chemical chaperoning by flavonoids: Structure?activity insights towards the design of potent amyloidosis inhibitors |pdf=|usr=}}{{29124175}} gab.com Text Transthyretin chemical chaperoning by flavonoids: Structure activity insights towards the design of potent amyloidosis inhibitors JO: Biochem Biophys Rep http://www.kidney.de/pget.php?&tw=1&pmid=29124175 #FOAvip Background: Many polyphenols have been proposed as broad-spectrum inhibitors of amyloid formation. To investigate structure?activity relationships relevant for the interaction of flavonoids with transthyretin (TTR), the protein associated with familial amyloid polyneuropathy (FAP), we compared the effects of major tea catechins and their larger polymers theaflavins, side-by-side, on TTR amyloid formation process. Methods: Interaction of flavonoids with TTR and effect on TTR stability were assessed through binding assays and isoelectric focusing in polyacrylamide gel. TTR aggregation was studied, in vitro, by dynamic light scattering (DLS), transmission electron microscopy (TEM) and in cell culture, through cytotoxicity assays. Results: Tested flavonoids bound to TTR and stabilized the TTR tetramer, with different potencies. The flavonoids also inhibited in vitro formation of TTR small oligomeric species and in cell culture inhibited pathways involving caspase-3 activation and ER stress that are induced by TTR oligomers. In all assays performed the galloyl esters presented higher potency to inhibit aggregation than the non-gallated flavonoids tested. Conclusions: Our results highlight the presence of gallate ester moiety as key structural feature of flavonoids in chemical chaperoning of TTR aggregation. Upon binding to the native tetramer, gallated flavonoids redirect the TTR amyloidogenic pathway into unstructured nontoxic aggregation assemblies more efficiently than their non-gallated forms. General significance: Our findings suggest that galloyl moieties greatly enhance flavonoid anti-amyloid chaperone activity and this should be taken into consideration in therapeutic candidate drug discovery. Twit Text FOAVip Transthyretin chemical chaperoning by flavonoids: Structure activity insights towards the design of potent amyloidosis inhibitors ????Biochem Biophys Rep http://www.kidney.de/pget.php?&tw=1&pmid=29124175 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29124175 #FOAvip English Wikipedia <ref>{{Cite pmid|29124175}}</ref> Transthyretin chemical chaperoning by flavonoids: Structure?activity insights towards the design of potent amyloidosis inhibitors #MMPMID29124175 Ferreira N; Pereira-Henriques A; Almeida MR Biochem Biophys Rep 2015[Sep]; 3 (ä): 123-33 PMID29124175show ga Background: Many polyphenols have been proposed as broad-spectrum inhibitors of amyloid formation. To investigate structure?activity relationships relevant for the interaction of flavonoids with transthyretin (TTR), the protein associated with familial amyloid polyneuropathy (FAP), we compared the effects of major tea catechins and their larger polymers theaflavins, side-by-side, on TTR amyloid formation process. Methods: Interaction of flavonoids with TTR and effect on TTR stability were assessed through binding assays and isoelectric focusing in polyacrylamide gel. TTR aggregation was studied, in vitro, by dynamic light scattering (DLS), transmission electron microscopy (TEM) and in cell culture, through cytotoxicity assays. Results: Tested flavonoids bound to TTR and stabilized the TTR tetramer, with different potencies. The flavonoids also inhibited in vitro formation of TTR small oligomeric species and in cell culture inhibited pathways involving caspase-3 activation and ER stress that are induced by TTR oligomers. In all assays performed the galloyl esters presented higher potency to inhibit aggregation than the non-gallated flavonoids tested. Conclusions: Our results highlight the presence of gallate ester moiety as key structural feature of flavonoids in chemical chaperoning of TTR aggregation. Upon binding to the native tetramer, gallated flavonoids redirect the TTR amyloidogenic pathway into unstructured nontoxic aggregation assemblies more efficiently than their non-gallated forms. General significance: Our findings suggest that galloyl moieties greatly enhance flavonoid anti-amyloid chaperone activity and this should be taken into consideration in therapeutic candidate drug discovery. äTransthyretin chemical chaperoning by flavonoids: Structure?activity i(epmc).pdf DeepDyve Pubget Overpricing