期刊
BIOORGANIC & MEDICINAL CHEMISTRY LETTERS
卷 23, 期 11, 页码 3438-3442出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmcl.2013.03.072
关键词
Phosphodiesterase 2 (PDE2) inhibition; Structure-based drug design; Osteoarthritis(OA) pain
We identified potent, selective PDE2 inhibitors by optimizing residual PDE2 activity in a series of PDE4 inhibitors, while simultaneously minimizing PDE4 activity. These newly designed PDE2 inhibitors bind to the PDE2 enzyme in a cGMP-like mode in contrast to the cAMP-like binding mode found in PDE4. Structure activity relationship studies coupled with an inhibitor bound crystal structure in the active site of the catalytic domain of PDE2 identified structural features required to minimize PDE4 inhibition while simultaneously maximizing PDE2 inhibition. (C) 2013 Elsevier Ltd. All rights reserved.
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