Title of article :
Interactions of leukocytes and platelets with poly(lysine/leucine) immobilized on tetraethylene glycol-terminated self-assembled monolayers
Author/Authors :
Martins، نويسنده , , M. Cristina L. and Ochoa-Mendes، نويسنده , , Vanessa and Ferreira، نويسنده , , Gisela and Barbosa، نويسنده , , Judite N. and Curtin، نويسنده , , Scott A. and Ratner، نويسنده , , Buddy D. and Barbosa، نويسنده , , Mلrio A. and Zagatto، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 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.
Keywords :
HEPARIN , Self-assembled monolayers , Surface charge , Platelets , Leukocytes
Journal title :
Acta Biomaterialia
Journal title :
Acta Biomaterialia