Abstract
This work investigates self-assembled monolayers that were formed from a glycol-terminated thiol monomer and were patterned using photoinduced monolayer desorption. Utilizing direct-write photolithography provided a facile means to generate complex protein patterns containing gradients and punctate regions. The ablated glycol monolayers were characterized using scanning probe microscopy, which allowed us to observe differences in the nanomechanical properties between the patterned and nonpatterned regions of the substrate. The patterned regions on the surface adsorbed proteins, and this process was monitored quantitatively using surface plasmon resonance imaging (SPRi). Moreover, the concentration of the protein could be controlled accurately by simply setting the gray level in the 8-bit image. Adsorbed protein was probed using a commercially available antibody binding assay, which showed significant enhancement over the background. The ability to produce complex protein patterns will contribute greatly to creating in vitro models that more accurately mimic an in vivo environment.
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