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Interactions of leukocytes and platelets with poly(lysine/leucine) immobilized on tetraethylene glycol-terminated self-assembled monolayers.

Authors :
Martins MC
Ochoa-Mendes V
Ferreira G
Barbosa JN
Curtin SA
Ratner BD
Barbosa MA
Source :
Acta biomaterialia [Acta Biomater] 2011 May; Vol. 7 (5), pp. 1949-55. Date of Electronic Publication: 2011 Jan 13.
Publication Year :
2011

Abstract

Surfaces that bind heparin are important for biomaterials for blood deheparinization. In our recent work it was demonstrated that a polypeptide composed of L-lysine and L-leucine (pKL), after immobilization onto tetra(ethylene glycol) terminated self-assembled monolayers (EG4-SAMs), can bind heparin from blood plasma in a selective, concentration-dependent way. During this work the effect of this peptide on platelet adhesion and activation and leukocyte adhesion was studied. The surface charge of these nanostructured surfaces was evaluated in order to correlate the effect of positively charged amine groups and hydrophobic methyl groups on the behavior of platelets and leukocyte adhesion. The results demonstrated that the presence of pKL decreased leukocyte adhesion to EG4-SAMs at all concentrations used. This effect is even more pronounced when surfaces were pre-immersed in heparinized plasma. In contrast, there is an increase in platelet adhesion and activation with increased percentage immobilized pKL. This effect is enhanced when surfaces were pre-immersed in heparinized plasma. However, adsorbed pKL in very low amounts does not induce platelet adhesion and activation compared with EG4, even when pre-immersed in plasma. Since only low pKL amounts are necessary to induce heparin selectivity, these results are promising for the development of heparin-binding biomaterials for blood deheparinization.<br /> (Copyright © 2011 Acta Materialia Inc. Published by Elsevier Ltd. All rights reserved.)

Details

Language :
English
ISSN :
1878-7568
Volume :
7
Issue :
5
Database :
MEDLINE
Journal :
Acta biomaterialia
Publication Type :
Academic Journal
Accession number :
21237292
Full Text :
https://doi.org/10.1016/j.actbio.2011.01.013