Immobilization of heparin on polysulfone surface for selective adsorption of low-density lipoprotein (LDL)
A versatile method was developed to immobilize heparin covalently on polysulfone sheets (PSu) to achieve selective adsorption of low-density lipoprotein (LDL). This was achieved by activation of PSu with successive treatments of chlorodimethyl ether and ethylenediamine, and subsequent chemical bindi...
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Published in | Acta biomaterialia Vol. 6; no. 3; pp. 1099 - 1106 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
England
Elsevier Ltd
01.03.2010
|
Subjects | |
Online Access | Get full text |
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Summary: | A versatile method was developed to immobilize heparin covalently on polysulfone sheets (PSu) to achieve selective adsorption of low-density lipoprotein (LDL). This was achieved by activation of PSu with successive treatments of chlorodimethyl ether and ethylenediamine, and subsequent chemical binding of heparin with bifunctional linker molecules. A heparin density up to 0.86
μg
cm
−2 on a dense PSu film was achieved. The modified PSu films were characterized by attenuated total reflectance Fourier transform infrared spectroscopy and X-ray photoelectron spectroscopy. The hydrophilicity of the PSu film was improved greatly by covalent immobilization of heparin. The water contact angle of PSu film was decreased from 86.6
±
3.7° to 50.5
±
3.2° after binding of 0.36
μg
cm
−2 heparin. An enzyme-linked immunosorbent assay was used to measure the binding of LDL on plain and modified PSu films. It was found that the heparin-modified PSu film could selectively recognize LDL from binary protein solutions. Furthermore, it was possible to desorb LDL from heparinized PSu, but not from plain PSu, with heparin, sodium chloride or urea solution, which indicates a selective but reversible binding of LDL to heparin. The results suggest that heparin-modified PSu membranes are promising for application in simultaneous hemodialysis and LDL apheresis therapy. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 1742-7061 1878-7568 |
DOI: | 10.1016/j.actbio.2009.08.039 |