Relationship between Structure and Papain Inhibitory Activity of Epoxysuccinyl Amino Acid Derivatives
- 1 March 1981
- journal article
- research article
- Published by Oxford University Press (OUP) in Agricultural and Biological Chemistry
- Vol. 45 (3) , 675-679
- https://doi.org/10.1080/00021369.1981.10864575
Abstract
A number of amino acid derivatives of DL-Zra/w-epoxysuccinic acid, with a general formula of R1O-ES-AA-OR2 (ES, DL-trans-epoxysuccinyl group; AA, amino acid residue) were newly synthesized and used for the study of structure-activity relationships of papain inhibition. Branched-alkyl amino acids, such as Leu, He and Val, as AA and hydrogen or an alkyl group substituted with a phenyl or cycloalkyl group as R1 were desirable for activity, respectively. However, R2 or the optical activities of ES and AA not so much influenced on the activity.This publication has 5 references indexed in Scilit:
- Purification and Properties of a New Cathepsin from Rat Liver1The Journal of Biochemistry, 1978
- Structure and Synthesis of E–64, a New Thiol Protease InhibitorAgricultural and Biological Chemistry, 1978
- Isolation and Characterization of E–64, a New Thiol Protease InhibitorAgricultural and Biological Chemistry, 1978
- Inhibitory Activities of E–64 Derivatives on PapainAgricultural and Biological Chemistry, 1978
- Further purification of a protease inhibitor from rabbit skin with healing inflammationBiochimica et Biophysica Acta (BBA) - General Subjects, 1965