In this research, films with compressive strength and aqueous stability were developed from camelina protein (CP) for tissue engineering. Protein based scaffolds have poor mechanical properties and aqueous stability and generally require chemical or physical modifications to make them applicable for medical applications. However, these modifications such as crosslinking could reduce biocompatibility and/or degradability of the scaffolds. Using proteins that are inherently water-stable could avoid modifications and provide scaffolds with the desired properties. CP with a high degree of disulfide cross-linkage has the potential to provide water-stable biomaterials, but it is difficult to dissolve CP and develop scaffolds. In this study, a new method of dissolving highly cross-linked proteins that results in limited hydrolysis and preserves the protein backbone was developed to produce water-stable films from CP without any modification. Only 12 % weight loss of camelina films was observed after 7 days in phosphate buffer saline (PBS) at 37°C. NIH 3T3 fibroblasts could attach and proliferate better on camelina films than on citric acid cross-linked collagen films. Therefore, CP films have the potential to be used for tissue engineering, and this extraction-dissolution method can be used for developing biomedical materials from various water-stable plant proteins.
Keywords: Camelina; aqueous stability; extraction-dissolution method; plant protein; tissue engineering scaffolds.
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