Title
An improved synthesis of haloaceteamidine-based inactivators of protein arginine deiminase 4 (PAD4)
UMMS Affiliation
Department of Biochemistry and Molecular Pharmacology
Publication Date
2008-07-07
Document Type
Article
Disciplines
Biochemistry | Enzymes and Coenzymes | Medicinal-Pharmaceutical Chemistry | Therapeutics
Abstract
Protein arginine deiminase 4 (PAD4) is an enzyme that hydrolyzes peptidyl arginine residues to form citrulline and ammonia. This enzyme has been implicated in several disease states, e.g. rheumatoid arthritis, and therefore represents a unique target for the development of a novel therapeutic. A solution-phase synthesis of Cl-amidine, the most potent PAD4 inactivator described to date, has been developed. This synthesis proceeds in 80% yield over 4 steps at a significantly (12-fold) lower cost.
DOI of Published Version
10.1016/j.tetlet.2008.05.021
Source
Tetrahedron Lett. 2008 Jul 7;49(28):4383-4385. Link to article on publisher's site
Journal/Book/Conference Title
Tetrahedron letters
Related Resources
Repository Citation
Causey, Corey P. and Thompson, Paul R., "An improved synthesis of haloaceteamidine-based inactivators of protein arginine deiminase 4 (PAD4)" (2008). Thompson Lab Publications. 68.
https://escholarship.umassmed.edu/thompson/68
Comments
At the time of publication, Paul Thompson was not yet affiliated with UMass Medical School.