Overview of recent drug discovery approaches for new generation leukotriene A(4) hydrolase inhibitors


ÇALIŞKAN B., BANOĞLU E.

EXPERT OPINION ON DRUG DISCOVERY, vol.8, no.1, pp.49-63, 2013 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Review
  • Volume: 8 Issue: 1
  • Publication Date: 2013
  • Doi Number: 10.1517/17460441.2013.735228
  • Journal Name: EXPERT OPINION ON DRUG DISCOVERY
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.49-63
  • Keywords: aminopeptidase, hydrolase, inflammation, leukotriene A4, leukotriene B4, PGP, BIFUNCTIONAL ENZYME, POTENT INHIBITORS, PHARMACOLOGICAL CHARACTERIZATION, 5-LIPOXYGENASE INHIBITOR, AMINOPEPTIDASE ACTIVITY, SELECTIVE INHIBITOR, CRYSTAL-STRUCTURE, LIPID MEDIATORS, ACID HCL, MECHANISMS
  • Gazi University Affiliated: Yes

Abstract

Introduction: LTA(4)H is a bifunctional enzyme with hydrolase and aminopeptidase activities. The hydrolase function of this enzyme specifically catalyzes the rate-limiting step in the conversion of LTA(4) to LTB4, one of the most potent chemoattractant and activator of neutrophils. The wealth of in vitro and in vivo data favors in support of LTA(4)H as an appealing target for the discovery and development of anti-inflammatory drugs.