title: Direct and reversible immobilization and microcontact printing of functional proteins on glass using a genetically appended silica-binding tag.
abstract: Fusion of disulfide-constrained or linear versions of the Car9 dodecapeptide to model fluorescent proteins support their on-contact and oriented immobilization onto unmodified glass. Bound proteins can be released and the surface regenerated by incubation with l-lysine. This noncovalent chemistry enables rapid and reversibe microcontact printing of tagged proteins and speeds up the production of bicontinuous protein patterns.
authors.affiliation: Department of Chemical Engineering, University of Washington, Box 351750, Seattle, WA, USA.
authors.forename: Brandon L
authors.initials: BL
authors.lastname: Coyle
authors.affiliation: Department of Chemical Engineering, University of Washington, Box 351750, Seattle, WA, USA.
authors.forename: François
authors.initials: F
authors.lastname: Baneyx
mesh_terms: D062028:Bioprinting; D004220:Disulfides / Q000737:chemistry; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000235:genetics; D005898:Glass / Q000737:chemistry*; D049452:Green Fluorescent Proteins / Q000737:chemistry / Q000235:genetics; D055767:Immobilized Proteins / Q000737:chemistry*; D008164:Luminescent Proteins / Q000737:chemistry / Q000235:genetics; D008239:Lysine / Q000737:chemistry; D010455:Peptides / Q000737:chemistry* / Q000235:genetics; D012822:Silicon Dioxide / Q000737:chemistry; D013879:Thioredoxins / Q000737:chemistry / Q000235:genetics; D000097573:Red Fluorescent Protein
chemical_list: D004220:Disulfides; D029968:Escherichia coli Proteins; D049452:Green Fluorescent Proteins; D055767:Immobilized Proteins; D008164:Luminescent Proteins; D008239:Lysine; D010455:Peptides; D012822:Silicon Dioxide; D013879:Thioredoxins; D000097573:Red Fluorescent Protein; C485184:enhanced green fluorescent protein