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10.1021/acs.langmuir.7b00527 http://scihub22266oqcxt.onion/10.1021/acs.langmuir.7b00527 C5489959!5489959!28558246     free     free     free Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Langmuir 2017 ; 33 (25): 6342-52 Nephropedia Template TP {{tp|p=28558246|t=2017. Buffers Strongly Modulate Fibrin Self-Assembly into Fibrous Networks |pdf=|usr=}}{{28558246}} gab.com Text Buffers Strongly Modulate Fibrin Self-Assembly into Fibrous Networks JO: Langmuir http://www.kidney.de/pget.php?&tw=1&pmid=28558246 #FOAvip Fibrin is a plasma protein with a central role in blood clotting and wound repair. Upon vascular injury, fibrin forms resilient fibrillar networks (clots) via a multistep self-assembly process, from monomers, to double-stranded protofibrils, to a branched network of thick fibers. In vitro, fibrin self-assembly is sensitive to physicochemical conditions like the solution pH and ionic strength, which tune the strength of the noncovalent driving forces. Here we report a surprising finding that the buffer?which is necessary to control the pH and is typically considered to be inert?also significantly influences fibrin self-assembly. We show by confocal microscopy and quantitative light scattering that various common buffering agents have no effect on the initial assembly of fibrin monomers into protofibrils but strongly hamper the subsequent lateral association of protofibrils into thicker fibers. We further find that the structural changes are independent of the molecular structure of the buffering agents as well as of the activation mechanism and even occur in fibrin networks formed from platelet-poor plasma. This buffer-mediated decrease in protofibril bundling results in a marked reduction in the permeability of fibrin networks but only weakly influences the elastic modulus of fibrin networks, providing a useful tuning parameter to independently control the elastic properties and the permeability of fibrin networks. Our work raises the possibility that fibrin assembly in vivo may be regulated by variations in the acute-phase levels of bicarbonate and phosphate, which act as physiological buffering agents of blood pH. Moreover, our findings add a new example of buffer-induced effects on biomolecular self-assembly to recent findings for a range of proteins and lipids. Twit Text FOAVip Buffers Strongly Modulate Fibrin Self-Assembly into Fibrous Networks ????Langmuir http://www.kidney.de/pget.php?&tw=1&pmid=28558246 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28558246 #FOAvip English Wikipedia <ref>{{Cite pmid|28558246}}</ref> Buffers Strongly Modulate Fibrin Self-Assembly into Fibrous Networks #MMPMID28558246 Kurniawan N; van Kempen THS; Sonneveld S; Rosalina TT; Vos BE; Jansen KA; Peters GWM; van de Vosse FN; Koenderink GH Langmuir 2017[Jun]; 33 (25): 6342-52 PMID28558246show ga Fibrin is a plasma protein with a central role in blood clotting and wound repair. Upon vascular injury, fibrin forms resilient fibrillar networks (clots) via a multistep self-assembly process, from monomers, to double-stranded protofibrils, to a branched network of thick fibers. In vitro, fibrin self-assembly is sensitive to physicochemical conditions like the solution pH and ionic strength, which tune the strength of the noncovalent driving forces. Here we report a surprising finding that the buffer?which is necessary to control the pH and is typically considered to be inert?also significantly influences fibrin self-assembly. We show by confocal microscopy and quantitative light scattering that various common buffering agents have no effect on the initial assembly of fibrin monomers into protofibrils but strongly hamper the subsequent lateral association of protofibrils into thicker fibers. We further find that the structural changes are independent of the molecular structure of the buffering agents as well as of the activation mechanism and even occur in fibrin networks formed from platelet-poor plasma. This buffer-mediated decrease in protofibril bundling results in a marked reduction in the permeability of fibrin networks but only weakly influences the elastic modulus of fibrin networks, providing a useful tuning parameter to independently control the elastic properties and the permeability of fibrin networks. Our work raises the possibility that fibrin assembly in vivo may be regulated by variations in the acute-phase levels of bicarbonate and phosphate, which act as physiological buffering agents of blood pH. Moreover, our findings add a new example of buffer-induced effects on biomolecular self-assembly to recent findings for a range of proteins and lipids. äBuffers Strongly Modulate Fibrin Self-Assembly into Fibrous Networks (epmc).pdf DeepDyve Pubget Overpricing