N-Benzoyl amino acids as LFA-1/ICAM inhibitors 1: amino acid structure–activity relationship

Bioorganic & Medicinal Chemistry Letters
2003.0

Abstract

The association of ICAM-1 with LFA-1 plays a critical role in several autoimmune diseases. N-2-Bromobenzoyl L-tryptophan, compound 1, was identified as an inhibitor to the formation of the LFA-1/ICAM complex. The SAR of the amino acid indicates that the carboxylic acid is required for inhibition and that L-histidine is the most favored amino acid.

Knowledge Graph

Similar Paper

N-Benzoyl amino acids as LFA-1/ICAM inhibitors 1: amino acid structure–activity relationship
Bioorganic & Medicinal Chemistry Letters 2003.0
Novel p-Arylthio Cinnamides as Antagonists of Leukocyte Function-Associated Antigen-1/Intracellular Adhesion Molecule-1 Interaction. 2. Mechanism of Inhibition and Structure-Based Improvement of Pharmaceutical Properties
Journal of Medicinal Chemistry 2001.0
New Cell-cell Adhesion Inhibitors from Streptomyces sp. UMA-044
The Journal of Antibiotics 2003.0
l-Type amino acid transporter 1 activity of 1,2,3-triazolyl analogs of l-histidine and l-tryptophan
Bioorganic & Medicinal Chemistry Letters 2019.0
Synthesis and biological activity evaluation of N-protected isatin derivatives as inhibitors of ICAM-1 expression on human endothelial cells
MedChemComm 2011.0
Angiotensin converting enzyme inhibitors. (Mercaptoaroyl)amino acids
Journal of Medicinal Chemistry 1985.0
N-Hydroxy-2-(naphthalene-2-ylsulfanyl)-acetamide, a novel hydroxamic acid-based inhibitor of aminopeptidase N and its anti-angiogenic activity
Bioorganic & Medicinal Chemistry Letters 2005.0
Structure-activity relationships for the inhibition of acrosin by benzamidine derivatives
Journal of Medicinal Chemistry 1978.0
Conformationally restricted arginine analogues as inhibitors of human nitric oxide synthase
Bioorganic & Medicinal Chemistry Letters 1997.0
LAT1 activity of carboxylic acid bioisosteres: Evaluation of hydroxamic acids as substrates
Bioorganic & Medicinal Chemistry Letters 2016.0