Logo image
Manipulation of kinetic profiles in 2-aryl propionic acid cyclooxygenase inhibitors
Journal article   Open access   Peer reviewed

Manipulation of kinetic profiles in 2-aryl propionic acid cyclooxygenase inhibitors

Kushol Gupta, Carl J Kaub, Kristen N Carey, Eduard G Casillas, Barry S Selinsky and Patrick J Loll
Bioorganic & medicinal chemistry letters, v 14(3), pp 667-671
2004
PMID: 14741265
url
https://doi.org/10.7270/q2n29wc9View
Open

Abstract

Slow tight-binding inhibitors NSAIDS Ibuprofen Flurbiprofen
The nonsteroidal anti-inflammatory drugs flurbiprofen and ibuprofen were modified in an attempt to alter the kinetics of inhibitor binding by COX-1. Contrary to prior predictions, a halogen substituent is not sufficient to confer slow tight-binding behavior. Conversion of the carboxylate moiety of flurbiprofen to an ester or amide abolishes slow tight-binding behavior, regardless of halogenation state. Structure–activity relationships are reported for compounds derived from the cyclooxygenase inhibitors flurbiprofen and ibuprofen, focusing on their kinetic profiles for COX-1 inhibition.

Metrics

11 Record Views
16 citations in Scopus

Details

UN Sustainable Development Goals (SDGs)

This publication has contributed to the advancement of the following goals:

#3 Good Health and Well-Being

InCites Highlights

Data related to this publication, from InCites Benchmarking & Analytics tool:

Collaboration types
Domestic collaboration
Web of Science research areas
Chemistry, Medicinal
Chemistry, Organic
Logo image