Insight into peculiar adhesion of cells to plasma-chemically prepared multifunctional "amino-glue" surfaces

Abstract

Plasma polymers (PPs) can easily modify material surfaces to improve their bio-applicability due to match-made surface-free energy and functionality. However, cell adhesion to PPs typically composed of various functional groups has not yet been fully understood. We explain the origin of strong resistance to trypsin treatment previously noted for nonendothelial cells on amine PPs. It is caused mainly by nonspecific adhesion of negatively charged parts of transmembrane proteins to the positively charged amine PP surface, enabled by thin glycocalyx. However, endothelial cells are bound primarily by their thick, negatively charged glycocalyx and sporadically by integrins in kinetic traps, both cleaved by trypsin. Cell scratching by atomic force microscopy tip confirmed the correlation of trypsin resistance to the strength of cell adhesion.Plasma polymers (PPs) can easily modify material surfaces to improve their bio-applicability due to match-made surface-free energy and functionality. However, cell adhesion to PPs typically composed of various functional groups has not yet been fully understood. We explain the origin of strong resistance to trypsin treatment previously noted for nonendothelial cells on amine PPs. It is caused mainly by nonspecific adhesion of negatively charged parts of transmembrane proteins to the positively charged amine PP surface, enabled by thin glycocalyx. However, endothelial cells are bound primarily by their thick, negatively charged glycocalyx and sporadically by integrins in kinetic traps, both cleaved by trypsin. Cell scratching by atomic force microscopy tip confirmed the correlation of trypsin resistance to the strength of cell adhesion.