Initial Cell Adhesion onto a Phospholipid Polymer Brush Surface Modified with a Terminal Cell Adhesion Peptide.

Dynamic changes in the properties of adsorbed protein layers at material surfaces make it difficult to analyze a cell adhesion behavior. Adhesion is affected by the ligand molecules in the adsorbed protein layers on the material's surface. This study aimed to quantitatively analyze the initial cell adhesion onto a polymeric surface modified with immobilized cell adhesion molecules with a well-defined structure. Peptides containing an arginine-glycine-aspartic acid (RGD) sequence were introduced at almost all the termini of the grafted poly(2-methacryloyloxyethyl phosphorylcholine) [poly(MPC)] chains using a click reaction at a highly protein-resistant poly(MPC) brush layer. Thus, the surface could bind to the cell membrane proteins only through the immobilized RGD. Furthermore, the degree of polymerization of the grafted poly(MPC) chains could control the hydrated poly(MPC) brush layer softness, as determined by measuring the dissipation energy loss using a quartz crystal microbalance. At the initial stage of cell adhesion, the density of cells adhering to the RGD-immobilized poly(MPC) brush layers did not depend on the poly(MPC) brush layer softness. However, spreading of the adherent cells was inhibited on the RGD-immobilized poly(MPC) brush layers with a higher softness. Hence, the results suggested that the layer softness did not affect the binding number between the RGD and cell membrane protein during initial cell adhesion; however, the intracellular signaling triggered by the RGD-receptor interaction was inhibited. The poly(MPC) brush surface carrying immobilized cell adhesion molecules has the potential to analyze precisely the effect of the properties of cell adhesion molecules on initial cell adhesion.