Structure-Guided Elaboration of a Fragment-Like Hit into an Orally Efficacious Leukotriene A4 Hydrolase Inhibitor-Reference-Cited by-同舟云学术

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Structure-Guided Elaboration of a Fragment-Like Hit into an Orally Efficacious Leukotriene A4 Hydrolase Inhibitor

Published:2024-03-13 Issue:6 Volume:67 Page:5093-5108
ISSN:0022-2623
Container-title:Journal of Medicinal Chemistry
language:en
Short-container-title:J. Med. Chem.

Author:

Thoma Gebhard¹^ORCID,Miltz Wolfgang¹,Srinivas Honnappa²,Penno Carlos A.²,Kiffe Michael³,Gajewska Monika³,Klein Kai³,Evans Amanda⁴,Beerli Christian⁴,Röhn Till A.⁴

Affiliation:

1. Global Discovery Chemistry, Biomedical Research, Novartis Pharma AG, 4002 Basel, Switzerland

2. Discovery Sciences, Biomedical Research, Novartis Pharma AG, 4002 Basel, Switzerland

3. PK Sciences, Biomedical Research, Novartis Pharma AG, 4002 Basel, Switzerland

4. Immunology Disease Area, Biomedical Research, Novartis Pharma AG, 4002 Basel, Switzerland

Funder

Novartis

Publisher

American Chemical Society (ACS)

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jmedchem.4c00290

Reference43 articles.

1. Leukotrien A4 hydrolase and the committed step in leukotriene B4 biosynthesis

2. Characterization of the aminopeptidase activity of epidermal leukotriene A4 hydrolase against the opioid dynorphin fragment 1-7

3. A Critical Role for LTA 4 H in Limiting Chronic Pulmonary Neutrophilic Inflammation

4. Opioid peptides are substrates for the bifunctional enzyme LTA4 hydrolase/aminopeptidase

5. Feasibility and physiological relevance of designing highly potent aminopeptidase-sparing leukotriene A4 hydrolase inhibitors

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