title: Two-component protein hydrogels assembled using an engineered disulfide-forming protein-ligand pair.
abstract: We present the development of a two-component self-assembling protein hydrogel. The building blocks of the hydrogel are two liquid-phase protein block copolymers each containing (1) a subunit of the trimeric protein CutA as a cross-linker and (2) one member of a PDZ-domain-containing protein-ligand pair whose interaction was reinforced by an engineered disulfide linkage. Mixing of the two building blocks reconstitutes a self-assembling polypeptide unit, triggering hydrogel formation. This hydrogel exhibits extremely high solution stability at neutral and acidic pHs and in a wide range of temperatures (4-50 °C). Incorporation of a "docking station peptide" binding motif into a hydrogel building block enables functionalization of the hydrogel with target proteins tagged with a "docking protein". We demonstrated the application of an enzyme-functionalized hydrogel in a direct electron transfer enzymatic biocathode. These disulfide-reinforced protein hydrogels provide a potential new material for diverse applications including industrial biocatalysis, biosynthesis, biofuels, tissue engineering, and controlled drug delivery.
authors.affiliation: Artie McFerrin Department of Chemical Engineering, Texas A&M University, College Station, 77843, United States.
authors.forename: Dongli
authors.initials: D
authors.lastname: Guan
authors.forename: Miguel
authors.initials: M
authors.lastname: Ramirez
authors.forename: Lin
authors.initials: L
authors.lastname: Shao
authors.forename: Daniel
authors.initials: D
authors.lastname: Jacobsen
authors.forename: Ivan
authors.initials: I
authors.lastname: Barrera
authors.forename: Jodie
authors.initials: J
authors.lastname: Lutkenhaus
authors.forename: Zhilei
authors.initials: Z
authors.lastname: Chen
mesh_terms: D019843:Archaeal Proteins / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry; D001674:Bioelectric Energy Sources; D002352:Carrier Proteins / Q000737:chemistry*; D003553:Cystine / Q000737:chemistry*; D004058:Diffusion; D004566:Electrodes; D004800:Enzymes, Immobilized / Q000737:chemistry; D006023:Glycoproteins / Q000737:chemistry*; D049452:Green Fluorescent Proteins / Q000737:chemistry; D020100:Hydrogels / Q000138:chemical synthesis*; D057927:Hydrophobic and Hydrophilic Interactions; D042845:Laccase / Q000737:chemistry; D008958:Models, Molecular; D016062:Porosity; D015202:Protein Engineering; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*; D014783:Viscosity; D018909:src Homology Domains
chemical_list: D019843:Archaeal Proteins; D001426:Bacterial Proteins; D002352:Carrier Proteins; D004800:Enzymes, Immobilized; D006023:Glycoproteins; D020100:Hydrogels; D029701:Saccharomyces cerevisiae Proteins; C070948:TIP1 protein, S cerevisiae; D049452:Green Fluorescent Proteins; D003553:Cystine; D042845:Laccase