Physical crosslinking modulates sustained drug release from recombinant silk-elastinlike protein polymer for ophthalmic applications.
Sequential block copolymers consisting of tandem repetition of amino acids have been constructed and genetically produced based on the natural repeating structures of silk and elastin protein. Combinations of silklike and elastinlike amino acid sequence blocks in a high molecular weight protein polymer are used to confer properties similar to those observed with hard block and soft block segmented polyurethanes. A certain subset of these silk-elastinlike protein compositions, termed ProLastins, will undergo an irreversible solution to gel transition in physiological, aqueous solution. The transition occurs over time and can be controlled by temperature, solution conditions, and additives which either prevent or promote hydrogen bond-mediated chain crystallization. The process involves no covalent crosslinking. Characterization of the gelling properties of various ProLastin compositions and their ability to release compounds which are incorporated directly into the gels are presented.