Sirisha Patchipulusu | PubMed Health

PubMed2004

Polymer cushions functionalized with lipid molecules.

This Letter reports a novel approach to the fabrication of a biomimicking surface by modification of an end-functionalizable smooth polymer cushion constructed via chemoselective ligation with a phospholipid-like molecule containing oxyamine groups. The mobility of a phospholipid bilayer formed by vesicle fusion on the phospholipid-like molecule terminated polymer film was characterized by fluorescence recovery after bleaching. Platelet adhesion, as one measure of biocompatibility of the film was also studied and compared to other surfaces such as polyethylene or poly(dimethylsiloxane). The results show that the end-functionalized smooth polymer cushion has potential as a biocompatible platform to reconstitute membrane proteins.

Fluorescence Recovery After Photobleaching↗

PubMedDate not supplied

In vitro flow evaluation of recombinant tissue factor pathway inhibitor immobilized on collagen impregnated Dacron.

Recombinant tissue factor pathway inhibitor (rTFPI) was immobilized on collagen impregnated (CI) knitted Dacron surfaces and its resistance to fibrin deposition evaluated following exposure to nonanticoagulated whole blood. Recombinant TFPI readily adsorbed to the CI Dacron surface and maintained its inhibitory activity. Under static conditions, rTFPI treated CI Dacron showed little fibrin deposition when compared with untreated surfaces. Treated samples exposed to flowing native blood at wall shear rates of 100 or 200 sec(-1) also demonstrated reduced fibrin deposition (up to 56%) compared with untreated samples. To assess the relative roles of the contact and tissue factor pathways in fibrin formation on artificial grafts, flow studies were performed with whole blood containing corn trypsin inhibitor, a potent inhibitor of FXIIa and contact activation. Corn trypsin inhibitor reduced fibrin deposition on untreated CI Dacron by 40%. Immobilized rTFPI alone, or corn trypsin inhibitor in combination with immobilized rTFPI, reduced fibrin deposition by 58% and 61%, respectively. These data suggest that immobilized rTFPI slows fibrin deposition on the vascular graft material by inhibiting both the contact pathway and blood borne tissue factor procoagulant activity arising from either the alternatively spliced form of tissue factor or from tissue factor containing microparticles.

Adsorption↗