Surfaces having dual fibrinolytic and protein resistant properties by immobilization of lysine on polyurethane through a PEG spacer
Hong Chen*, Yanxia Zhang, Dan Li, Xiaoyang Hu, Liang Wang, W. Glenn Mcclung, John L. Brash. Journal of Biomedical Materials Research:Part A, 2009, 0, 940-946.
文章链接:http://dx.doi.org/10.1002/jbm.a.32152

The objective of this work is to develop a blood contacting surface that possesses both resistance to nonspecific protein adsorption and clot lysing properties. Chemical modification of a polyurethane (PU) surface with poly(ethylene glycol) (PEG); and lysine was used to create a plasminogen- binding potentially fibrinolytic surface. The preparation involves modification of the PU surface with dihydroxyPEG, reaction of the unreacted distal OH with N,N0-disuccinimidyl carbonate (DSC) to produce a PU-PEG-NHS surface,followed by conjugation of e-amino-protected lysine (H-Lys(t-BOC)-OH) by reaction of the a-amino group with the NHS and deprotection. The result is a lysine derivatized surface in which the e-amino groups of the lysine are free to participate in binding plasminogen and tissue plasminogen
activator (t-PA). Surfaces were characterized by X-ray photoelectron spectroscopy (XPS) and contact angle measurements. Protein adsorption experiments showed that nonspecific protein adsorption was greatly reduced on these surfaces and that they adsorbed significant quantities of plasminogen from plasma. After incubation with plasma and treatment with t-PA the surfaces were able to dissolve nascent plasma clots formed around them.



 

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