Free-formed submicron-fabrication of protein matrix via multiphoton photochemical crosslinking

Abstract

Photochemical crosslinking is effective in enhancing long-term stability of protein (e.g. collagen and fibronectin) structures without compromising the tissue compatibility. In this work, multiphoton-based photochemical crosslinking was used to fabricate protein structures with micron- and sub-micron-sized structures using bovine serum albumin (BSA) as the sample protein and rose Bengal (RB) as the photosensitizer. Our ultimate goal is to study how cells respond to patterned structures with sub-micron sized topological features. Arrays of BSA micro-pillars have been fabricated. Excellent 3D resolution in defining the shape of micro-pillar structures, either pyramidal or conical, was achieved by precisely controlling various scanning parameters and solution concentrations. The morphology of the protein structures fabricated was evaluated by multi-photon confocal microscopy and scanning electron microscopy (SEM).