97885-48-8Relevant articles and documents
A molecular probe with both chromogenic and fluorescent units for detecting serine proteases
Ishida, Kirara,Nakamura, Yushi,Oe, Yohei,Ohta, Tetsuo
, (2021/06/18)
A molecular probe with L-phenylalanine p-nitroanilide and L-lysin 4-methylcoumaryl-7-amide, in which these amino acid derivatives are connected through a succinic-acid spacer, was prepared. Trypsin and papain were detected by blue-fluorescence emission of generated 7-amino-4-methylcoumarin (AMC). α-Chymotrypsin and nattokinase were detected from both the blue-fluorescence emission of AMC and the UV absorbance of p-nitroaniline. In addition, different time courses of p-nitroaniline and AMC were observed between the reaction of P1 with α-chymotrypsin and that with nattokinase. In the case of nattokinase, both the fluorescence emission and UV absorbance slowly increased. In contrast, the increasing UV absorbance was saturated at the early stage of the reaction of the present probe with chymotrypsin, whereas the fluorescence emission continuously increased in the following stages.
Amidase activity of phosphonate analogue imprinted chymotrypsin mimics in shape-selective, substrate-specific and enantioselective amidolysis of l-phenylalanine-p-nitroanilides
Mathew, Divya,Thomas, Benny,Devaky
, p. 65 - 73 (2016/02/18)
Focusing on chymotrypsin mimics, highly crosslinked enzyme mimics are synthesized by molecular imprinting technique for the amidolysis of p-nitroanilide of phenylalanine, using phenyl-1-(N-benzyloxycarbonylamino)-2-(phenyl)ethyl phosphonate - the transition state analog of amidolysis - as the template, N-methacryloyl-l-histidine, N-methacryloyl-l-aspartic acid, and N-methacryloyl-l-serine as the functional monomers and EGDMA as the crosslinking agent. The amidase activity of the enzyme mimics follows pseudo first order kinetics. The transition state analog provides a tetrahedral geometry complementary to the transition state intermediate, which is responsible for the catalytic activity of the imprinted enzyme mimics. The enzyme mimics show stereospecificity and substrate selectivity in the amidolysis of phenylalanine p-nitroanilide. The proper orientation of the reactive functionalities in the super crosslinked macroporous polymer matrix for selective binding of the substrate through H-bonding is responsible for the high imprinting efficiency and substrate specificity of the imprinted polymer catalysts. Low cost, ease of preparation, high thermal stability, reusability and higher shelf life make the polymer catalysts better chymotrypsin mimics.
An efficient synthesis of Nα-protected amino and peptide acid aryl amides via iodine-mediated oxidative acylation of N α-protected amino and peptide thioacids
Madhu, Chilakapati,Vishwanatha,Sureshbabu, Vommina V.
, p. 2727 - 2736 (2013/10/21)
Thioacids derived from N-protected amino or dipeptide and tripeptide acids undergo facile N-acylation with aromatic amines to afford N-protected amino or peptide aryl amides in good to excellent yields and enantiopurities. The method also furnishes difficult-to-prepare N-Fmoc amino acid 4-nitroanilides in good yields. This simple oxidative Nα-acylation of thioacids with aromatic amines proceeds in the presence of iodine, 1-hydroxybenzotriazole and N,N-diisopropylethylamine at room temperature in tetrahydrofuran. Georg Thieme Verlag Stuttgart New York.
