Potent inhibition of Ca2+-dependent activation of calpain-1 by novel mercaptoacrylates

Adams, Sarah Elizabeth, Parr, Christian, Miller, David James, Allemann, Rudolf Konrad ORCID: https://orcid.org/0000-0002-1323-8830 and Hallett, Maurice Bartlett ORCID: https://orcid.org/0000-0001-8197-834X 2012. Potent inhibition of Ca2+-dependent activation of calpain-1 by novel mercaptoacrylates. MedChemComm 3 (5) , pp. 566-570. 10.1039/c2md00280a

Full text not available from this repository.

Abstract

Calpain-1 is a Ca2+-activated cytosolic cysteine protease. Its activation has been linked to extravasation into inflamed tissue of white blood cells, especially neutrophils. Calpain-1 may therefore be an anti-inflammatory target for therapeutic intervention. 24 novel monohalogenated phenyl and indole mercaptoacrylic acid derivatives were synthesised. The location and nature of the ring-coupled halides strongly influenced the potency of these compounds to inhibit calpain activation. Several of the calpain-1 inhibitors showed IC50 values in the low nanomolar range and prevented cell shape change of neutrophils, a necessary prelude to their migration from the blood in the body.

Item Type:	Article
Status:	Published
Schools:	Schools > Chemistry Research Institutes & Centres > Cardiff Catalysis Institute (CCI)
Subjects:	Q Science > QD Chemistry
Publisher:	RSC Publishing
ISSN:	2040-2503
Funders:	EPSRC, MRC
Last Modified:	20 Oct 2022 08:07
URI:	https://orca.cardiff.ac.uk/id/eprint/27318

Citation Data

Cited 22 times in Scopus. View in Scopus. Powered By Scopus® Data

Actions (repository staff only)

Edit Item