A protein-cleaving catalyst specific for a disease-related protein can be used as a catalytic drug. As the first protein-cleaving catalyst selective for a protein substrate, a catalyst for myoglobin was designed by attaching Cu(II) or Co(III) complex of cyclen to a binding site searched by a combinatorial method using peptide nucleic acid monomers as building units. [reaction: see text]

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Eight title compounds of type (I) or (II) are prepared as diastereomeric mixtures which can be separated by HPLC. The Cu(II) and Co(III) complexes of the isomers of (I) and (II) with the longer elution time contain an effective binding site for carboxypeptidase A (CPA) as well as the peptide-cleaving catalytic center, but they fail to cleave the peptide backbone of CPA. -(SONG, J. B.; HAH, S. S.; SUH*, J.; Bull. Korean Chem.

Highly efficient WOLEDs, with the efficiencies of 19 cd/A, 16 cd/A, and 33 cd/A and CIE color coordinates of (0.25, 0.35), (0.30, 0.32), and (0.30, 0.32) respectively, have been developed. The broad white emitting TE‐WOLEDs for high resolution display have been realized by controlling the microcavity between the cathode and anode. 96 % of NTSCx,y ratio was achieved from the TE‐WOLED with the optical path control layer (OPCL) and new green color filter (CF).