We have created polymer/peptide multiblock hybrid copolymers containing multiple repeats of functional peptides derived from the natural proteins as protein mimetics for biomedical applications. For example, elastin mimetic hybrid polymers (EMHPs) composed of poly(ethylene glycol) (PEG) alternating with an alanine-rich, lysine-containing peptide [(AKA3KA)2, AK2], with or without the cell-binding domains, were synthesized by condensation polymerization employing copper (I) catalyzed alyne-azide cycloaddition (CuAAC) reaction. Covalent crosslinking of [PEG-AK2]n through the lysine amines afforded cell-adhesive, elastomeric hydrogels.Separately, EMHPs consisting of poly(acrylic acid) (PAA) alternating with a elastin-based peptide [(VPGVG)2, VG2] have also been successfully synthesized under CuAAC conditions. [PAA-VG2]n self-assembled into discrete nanoparticles through the concerted interactions between the constituent building blocks. Recently, tetrazine ligation, an ultrafast cycloaddition of s-tetrazine (Tz) with trans-cyclooctene (TCO) derivatives, was employed for the synthesis of multiblock copolymers using homo-difunctional Tz and TCO derivatives via an interfacial polymerization process. As the polymerization proceeded, high molecular weight polymer fibers were pulled out of the interface. Introduction of peptidic building block in the monomer mixture resulted in a quantitative incorporation of the peptide in the resultant copolymers ([PEG-C12(RGD)]n). The modular approaches allow facile substitution of the polymer and peptide segments to fine-tune the materials properties for applications in tissue engineering and drug delivery.

Tunable multiblock hybrid copolymers as protein mimetics

248th National Meeting (2014)

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