Abstract: The present disclosure provides synthetic collagen and methods of making and using synthetic collagen that include a synthetic collagen that facilitates wound closure comprising an isolated and purified triple helical backbone protein that facilitates wound closure comprising one or more alteration in a triple helical backbone protein sequence, that stabilize the isolated and purified triple helical backbone protein and does not disrupt an additional collagen ligand interaction; and one or more integrin binding motifs, wherein the isolated and purified triple helical backbone protein facilitates wound closure.

Abstract: An improved polymer delivery system is described which provides polymeric microparticle compositions and porous microparticles formed therefrom. Pore size, pore architecture as well as particle size are also controllable. In some embodiments, both the polymeric microparticle compositions and porous microparticles formed therefrom encapsulate at least one substance, such as a biologic substance (one having biologic activity and/or compatible with a biologic system). The encapsulation occurs prior to polymerization. The amount of substance that is encapsulated may be controlled by the described methods. Said methods do not emply organic solvents. As such, the fabrication occurs in a solvent-free system.

Abstract: The present disclosure provides synthetic collagen and methods of making and using synthetic collagen that include a synthetic collagen that facilitates wound closure comprising an isolated and purified triple helical backbone protein that facilitates wound closure comprising one or more alteration in a triple helical backbone protein sequence, that stabilize the isolated and purified triple helical backbone protein and does not disrupt an additional collagen ligand interaction; and one or more integrin binding motifs, wherein the isolated and purified triple helical backbone protein facilitates wound closure.

Abstract: The present disclosure provides synthetic collagen and methods of making and using synthetic collagen that include a synthetic collagen that facilitates wound closure comprising an isolated and purified triple helical backbone protein that facilitates wound closure comprising one or more alteration in a triple helical backbone protein sequence, that stabilize the isolated and purified triple helical backbone protein and does not disrupt an additional collagen ligand interaction; and one or more integrin binding motifs, wherein the isolated and purified triple helical backbone protein facilitates wound closure.

Abstract: An improved polymer delivery system is described which provides polymeric microparticle compositions and porous microparticles formed therefrom. Pore size, pore architecture as well as particle size are also controllable. In some embodiments, both the polymeric microparticle compositions and porous microparticles formed therefrom encapsulate at least one substance, such as a biologic substance (one having biologic activity and/or compatible with a biologic system). The encapsulation occurs prior to polymerization. The amount of substance that is encapsulated may be controlled by the described methods. Said methods do not emply organic solvents. As such, the fabrication occurs in a solvent-free system.

Abstract: High internal phase emulsions (HIPEs) and polyHIPEs formed therefrom. HIPE components have been adjusted to delay and/or prevent polymerization and free radical decomposition at certain temperatures. Methods include preparing two water-in-oil emulsions; one emulsion includes an oxidizing initiator at a concentration not sufficient to induce polymerization, and another emulsion includes a reducing agent. The two emulsions may be stored for months. When combined, a redox reaction is induced, resulting in polymerization (polyHIPE formation) at temperatures below 100° C., such as between 20° C. and 40° C. This allows a final composition to be formed in situ, with or without highly sensitive materials, including biologically-derived or active constituents (e.g., cells, growth factors, enzymes, proteins, drugs, chemoactive agents). The polymerization rate may be short, as fast as thirty seconds.

Abstract: Materials and methods for preparing three dimensional scaffolds are described. The materials, as improved high internal phase emulsions (HIPES), and the polymerization thereof may be suitable for injection prior to curing and when in an injectable form may be for site-directed in vivo use, curing after injection. In addition, said materials before curing may be engineered as a tissue substitution or enhancement and/or to include cell encapsulation. Said materials described herein form a monolith after curing and are biodegradable and porous after curing. Said materials are made from starting molecules using a process that does not rely on toxic solvents or monomers. Making of said materials to form the emulsion take advantage of one or more surfactants for HIPE stability. In addition, said materials cure at temperatures appropriate for use in an in vivo or in situ environment.

Abstract: The present disclosure provides synthetic collagen and methods of making and using synthetic collagen that include a synthetic collagen that facilitates wound closure comprising an isolated and purified triple helical backbone protein that facilitates wound closure comprising one or more alteration in a triple helical backbone protein sequence, that stabilize the isolated and purified triple helical backbone protein and does not disrupt an additional collagen ligand interaction; and one or more integrin binding motifs, wherein the isolated and purified triple helical backbone protein facilitates wound closure.

Abstract: The present invention identified a recombinant synthetic collagen containing a triple helical backbone protein produced in a prokaryotic expression system where the protein contains at least one ‘inserted’ biologically active sequence(s).

Abstract: The present invention identified a recombinant synthetic collagen containing a triple helical backbone protein produced in a prokaryotic expression system where the protein contains at least one ‘inserted’ biologically active sequence(s).