Protein-engineered biomaterials: highly tunable tissue engineering scaffolds.
A common goal in tissue engineering is to attain the ability to tailor specific cell-scaffold interactions and thereby gain control over cell behavior. The tunable nature of protein-engineered biomaterials enables independent tailoring of a range of biomaterial properties, creating an attractive alternative to synthetic polymeric scaffolds or harvested natural scaffolds. Protein-engineered biomaterials are comprised of modular peptide domains with various functionalities that are encoded into a DNA plasmid, transfected into an organism of choice, and expressed and purified to yield a biopolymer with exact molecular-level sequence specification. Because of the modular design strategy of protein-engineered biomaterials, these scaffolds can be easily modified to enable optimization for specific tissue engineering applications. By including multiple peptide domains with different functionalities in a single, modular biomaterial, the scaffolds can be designed to mimic the diverse properties of the natural extracellular matrix, including cell adhesion, cell signaling, elasticity, and biodegradability. Recently, the field of protein-engineered biomaterials has expanded to include functional modules that are not normally present in the extracellular matrix, thus expanding the scope and functionality of these materials. For example, these modules can include noncanonical amino acids, inorganic-binding domains, and DNA-binding sequences. The modularity, tunability, and sequence specificity of protein-engineered biomaterials make them attractive candidates for use as substrates for a variety of tissue engineering applications.
Department of Chemistry, Stanford University, Stanford, California 94305, USA.
Debanti
D
Sengupta
Sarah C
SC
Heilshorn
D001672:Biocompatible Materials / Q000138:chemical synthesis*; D001704:Biopolymers / Q000096:biosynthesis / Q000737:chemistry; D006801:Humans; D008954:Models, Biological; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000737:chemistry; D015202:Protein Engineering / Q000379:methods*; D011506:Proteins / Q000737:chemistry*; D023822:Tissue Engineering / Q000379:methods
D001672:Biocompatible Materials; D001704:Biopolymers; D010446:Peptide Fragments; D011506:Proteins