Functional Biomaterials: Elastin-Mimetic Hybrid Polymers
Elastin is a natural polypeptide with distinct elastomeric properties. Elastin achieves its excellent mechanical properties through a multiblock copolypeptide structure composed largely of two types of short segments that alternate along the polypeptide chain: highly flexible hydrophobic segments composed of VPGVG repeats, with many transient structures that can easily change their conformation when stretched; and alanine- and lysine- rich alpha-helical segments, which form crosslinks between adjacent molecules via the action of lysyl oxidase in the ECM.
Intrigued by the entropic origin of elastin elasticity, we have been engaged in developing multiblock peptide-polymer hybrid polymers consisting of hydrophobic flexible synthetic polymer alternating with alanine-rich peptides that are the structural component of the hydrophilic crosslinking domain of the natural elastin. These hybrid polymers were constructed by condensation polymerization via Orthogonal Click Chemistry using flexible synthetic polymers and alanine-rich, lysine-containing peptides as the building blocks. Subsequent covalent cross-linking of the pre-registered lysin residue led to a strong and elastomeric hydrogels.
1. Grieshaber, S. E.; Farran, A. J. E.; Lin-Gibson, S.; Kiick, K. L.; Jia, X.* "Synthesis and Characterization of Elastin-Mimetic Hybrid Polymers with Multiblock, Alternating Molecular Architecture and Elastomeric Properties" Macromolecules, 2009, 42, 2532-2541.
2. Jia, X.*; Kiick, K. L.; "Hybrid Multicomponent Hydrogels for Tissue Engineering" Macromol. Biosci., 2009, 9, 140-156.