Endothelial cell adhesion and blood response to hemocompatible peptide 1 (HCP-1), REDV, and RGD peptide sequences with free N-terminal amino groups immobilized on a biomedical expanded polytetrafluorethylene surface.

Blood compatibility generally requires two contradictory characteristics: reduced protein/platelet adhesion and excellent endothelium-related cell affinity. To understand the effect of cell adhesion peptides on blood compatibility, the peptides REDV, RGD, and hemocompatible peptide-1 (HCP-1) were immobilized on an expanded polytetrafluorethylene (ePTFE) surface and evaluated in vitro, in situ, and in vivo. Since the terminal amino groups of functional peptides often have an important effect, a cysteine residue was added to the C terminal and used for immobilization to keep the terminal amino groups free. Maleimide groups were added to carboxylic groups of highly hydrophilic and biologically inert (bioinert) polymer chains grafted onto ePTFE and coupled with cysteine residues. In vitro tests revealed that free N-terminal HCP-1 and RGD-immobilized surfaces improved the adhesion and spread of human umbilical vein endothelial cells (HUVECs), while, unexpectedly, a free N-terminal adjacent to REDV suppressed cell affinity. In situ evaluation with a porcine closed-circuit system for 2 h showed that no platelets adhered to the modified ePTFE sutures due to the bioinert graft chain containing phosphorylcholine groups. Simultaneously, leukocyte-related and endothelium-related cells were observed on RGD-immobilized ePTFE sutures because RGD was recognized by broad types of cells. These cells were not observed on the HCP-1- and REDV-immobilized ePTFE sutures, which may be due to insufficient exposure time. HCP-1-modified ePTFE graft implantation in a porcine femorofemoral (FF) bypass model for 10 days showed that the thrombus layer was clearly mitigated by HCP-1 immobilization. This study suggests that the HCP-1-immobilized ePTFE surface has potential for long-term application by mitigating thrombus and supporting endothelial cell adhesion.