Effect of Functional Groups of Self-Assembled Monolayers on Protein Adsorption and Initial Cell Adhesion

Surface modification plays a vital role in regulating protein adsorption and subsequently cell adhesion. In the present work, we prepared nanoscaled modified surfaces using silanization and characterized them using Fourier-transform infrared spectroscopy (FTIR), water contact angle (WCA), and atomic force microscopy (AFM). Five different (amine, octyl, mixed, hybrid, and COOH) surfaces were prepared based on their functionality and varying wettability and their effect on protein adsorption and initial cell adhesion was investigated. AFM analysis revealed nanoscale roughness on all modified surfaces. Fetal bovine serum (FBS) was used for protein adsorption experiment and effect of FBS was analyzed on initial cell adhesion kinetics (up to 6 h) under three different experimental conditions: (a) with FBS in media, (b) with preadsorbed FBS on surfaces, and (c) incomplete media, i.e., without FBS. Various cell features such as cell morphology/circularity, cell area and nuclei size were also studied for the above stated conditions at different time intervals. The cell adhesion rate as well as cell spread area were highest in the case of surfaces with preadsorbed FBS. We observed higher surface coverage rate by adhering cells on hybrid (rate, 0.073 h –1 ) and amine (0.072 h –1 ) surfaces followed by COOH (0.062 h –1 ) and other surfaces under preadsorbed FBS condition. Surface treated with cells in incomplete media exhibited least adhesion rate, poor cell spreading and improper morphology. Furthermore, we found that initial cell adhesion rate and Δ a dhered cells (%) linearly increased with the change in α-helix content of adsorbed FBS on surfaces. Among all the modified surfaces and under all three experimental conditions, hybrid surface exhibited excellent properties for supporting cell adhesion and growth and hence can be potentially used as surface modifiers in biomedical applications to design biocompatible surfaces.