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Cover Feature: Characterisation of the Carboxypeptidase G2 Catalytic Site and Design of New Inhibitors for Cancer Therapy (ChemBioChem 18/2018)
Author(s) -
Jeyaharan Dhadchayini,
Brackstone Carla,
Schouten James,
Davis Paul,
Dixon Ann M.
Publication year - 2018
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201800490
Subject(s) - prodrug , adept , conjugate , active site , chemistry , enzyme , cancer therapy , pharmacology , drug , biochemistry , cancer , combinatorial chemistry , medicine , mathematical analysis , mathematics
The cover feature picture shows the binding of a new inhibitor to the CPG2 enzyme to prevent off‐site generation of an active drug as part of antibody‐directed enzyme prodrug therapy (ADEPT). ADEPT involves administration of an enzyme–antibody conjugate directed at tumor‐associated antigens, followed by administration of a prodrug that is enzymatically converted to its active form at the tumor site. This approach reduces the toxic effects of cancer therapy, but requires inhibition and clearance from circulation of any unbound conjugate ahead of administration of the prodrug. It is this goal that is the focus of the full paper by A. M. Dixon et al. on page 1959 in Issue 18, 2018 (DOI: 10.1002/cbic.201800186).