@article{8a9873697e874ebe847f0a85742fb2f2,
title = "Synthesis and evaluation of aminophosphinic acid derivatives as inhibitors of renal dipeptidase",
abstract = "Renal dipeptidase (RDP) is an enzyme overexpressed in benign and malignant colorectal tumors. In an effort to identify potent inhibitors of this enzyme, a series of aminophosphinic acid derivatives were synthesized. Compounds 3a and 3c in which the phenyl ring was para substituted with F and Br and olefin with Z geometry, showed better inhibitory activity against RDP enzyme (IC 50=5-6nM).",
keywords = "Aminophosphinic acid derivatives, RDP inhibitors",
author = "Hallur Gurulingappa and Phillip Buckhalts and Kinzler, {Kenneth W.} and Bert Vogelstein and Khan, {Saeed R.}",
note = "Funding Information: We are grateful for the support provided by the National Institute of Health (CA 62924) and an intramural grant from the Maryland Cigarette Restitution Fund and FAMRI to S.R.K. We thank the Biophysical Chemistry Department for NMR studies. K.W.K. receives research funding from Genzyme Molecular Oncology (Genzyme). Under a licensing agreement between the Johns Hopkins University and Genzyme, RDP-based technology is licensed to Genzyme, and K.W.K. and B.V. are entitled to a share of royalty received by the University from sales of the licensed technology. The terms of these arrangements are being managed by the University in accordance with its conflict of interest policies.",
year = "2004",
month = jul,
day = "5",
doi = "10.1016/j.bmcl.2004.04.057",
language = "English (US)",
volume = "14",
pages = "3531--3533",
journal = "Bioorganic and Medicinal Chemistry Letters",
issn = "0960-894X",
publisher = "Elsevier Limited",
number = "13",
}