| 摘要 |
The present invention concerns the synthesis of an artificial glycosyl hydrolase enzyme, comprising an active site capable of bifunctional catalysis, which has been covalently bonded to a rigid organic matrix through the use of a tethering construct. The active site of this enzyme can comprise natural amino acids, unnatural amino acids, which include enantiomers, disastereomers, or homologues of a natural amino acid, or peptidomimetic amino acids that contain a catalytic moiety typically found on an amino acid, including carboxylic acid, hydroxyl, thiol, amine, amide, guanidinyl, imidazoyl, selenyl, or aryl. Other non-biotic groups known to participate in glycosidic bond cleavage include urea and thiourea. The rigid organic matrix of this artificial enzyme comprises a singularity or plurality of biopolymeric matrices, including deoxyribonucleic acid, ribonucleic acid, locked nucleic acid, morpholino nucleic acid, or peptide nucleic acid helices or helical bundles. The unique chemical function can comprise glycosidic bond hydrolysis using a bifunctional catalytic mechanism. |
