Artificial polypeptide scaffold for protein immobilization.
An artificial polypeptide scaffold composed of surface anchor and protein capture domains was designed and expressed in vivo. By using a mutant E. coli phenylalanyl-tRNA synthetase, the photoreactive amino acid para-azidophenylalanine was incorporated into the surface anchor domain. Octyltrichlorosilane-treated surfaces were functionalized with this polypeptide by spin coating and photocrosslinking. The resulting protein films were shown to immobilize recombinant proteins through association of coiled coil heterodimer.
Zhang
Kechun
K
Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California 91125, USA.
Diehl
Michael R
MR
Tirrell
David A
DA
D000595:Amino Acid Sequence; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics / Q000378:metabolism; D005982:Glutathione Transferase / Q000737:chemistry; D049452:Green Fluorescent Proteins / Q000737:chemistry; D016350:Leucine Zippers; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D010652:Phenylalanine-tRNA Ligase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D040081:Protein Array Analysis / Q000379:methods*; D011994:Recombinant Proteins / Q000737:chemistry*; D012821:Silanes / Q000737:chemistry
D010455:Peptides; D011994:Recombinant Proteins; D012821:Silanes; D049452:Green Fluorescent Proteins; D005982:Glutathione Transferase; D010652:Phenylalanine-tRNA Ligase; C025249:octyltrichlorosilane