## Abstract Using the layer‐by‐layer technique, ELISA polystyrene plates were coated with multilayer assemblies of albumin with various heparins or with multilayer assemblies of albumin. The coatings containing heparin were tested for their ability to potentiate thrombin inhibition by antithrombin
In vitro hemocompatibility of albumin–heparin multilayer coatings on polyethersulfone prepared by the layer-by-layer technique
✍ Scribed by Claudia Sperling; Milan Houska; Eduard Brynda; Uwe Streller; Carsten Werner
- Publisher
- John Wiley and Sons
- Year
- 2006
- Tongue
- English
- Weight
- 262 KB
- Volume
- 76A
- Category
- Article
- ISSN
- 1549-3296
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✦ Synopsis
Abstract
Polyethersulfone foils (PES)—a unique material for blood purification membranes—were coated with a multilayer assembly of heparin (unfractionated or high anticoagulant activity fraction heparin) and albumin (albumin–heparin coatings), or with a multilayer of albumin (albumin coating), using the layer‐by‐layer technique. The coatings combine advantages of albumin (reduction of nonspecific interactions) and heparin (specific interactions with blood coagulation proteins). The differences between the two heparins, while significant for their biological activity, had only a minor effect on the multilayer assembly with albumin monitored in situ by reflection infrared spectroscopy (FTIR MIRS). Uncoated as well as modified PES surfaces were evaluated using an in vitro assay with freshly drawn, slightly heparinized (1.5 IU heparin/mL) human whole blood. The blood was circulated with a roller pump over the sample surfaces in shear flow across rectangular slit channels (
app. 6 mL/min and
120 s^−1^) for 1.5 h at 37°C. All coatings effectively reduced platelet adhesion and activation according to the PF4 release. The activation of coagulation evaluated as TAT generation was significantly lowered for the coating composed of albumin and high activity heparin. A further beneficial effect of the heparin containing coatings was reduced complement activation as determined by different complement fragments. © 2005 Wiley Periodicals, Inc. J Biomed Mater Res, 2006
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