93434-59-4Relevant articles and documents
Selective Monovalent Galectin-8 Ligands Based on 3-Lactoylgalactoside
Anderluh, Marko,Girardi, Benedetta,Leffler, Hakon,Manna, Martina,Mravljak, Janez,Nilsson, Ulf J.,Ricklin, Daniel,Schwardt, Oliver,Van Klaveren, Sjors,Jakopin, ?iga,Toma?i?, Tihomir
supporting information, (2021/10/08)
Galectin-8 has gained attention as a potential new pharmacological target for the treatment of various diseases, including cancer, inflammation, and disorders associated with bone mass reduction. To that end, new molecular probes are needed in order to better understand its role and its functions. Herein we aimed to improve the affinity and target selectivity of a recently published galectin-8 ligand, 3-O-[1-carboxyethyl]-β-d-galactopyranoside, by introducing modifications at positions 1 and 3 of the galactose. Affinity data measured by fluorescence polarization show that the most potent compound reached a KD of 12 μM. Furthermore, reasonable selectivity versus other galectins was achieved, making the highlighted compound a promising lead for the development of new selective and potent ligands for galectin-8 as molecular probes to examine the protein's role in cell-based and in vivo studies.
ENDOPARASITIC DEPSIPEPTIDES
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Page/Page column 44; 48, (2019/11/28)
The present invention provides cyclic depsipeptides of Formula (1), stereoisomers thereof, and veterinary acceptable salts thereof wherein each of R1, R2, R3, R4, L1, and L2 are as defined herein. The present invention also contemplates compositions, methods of treatment, and uses as a medicament to treat an animal for an endoparasitic infection with a Formula (1 ) compound.
Total synthesis of the cyclic depsipeptide YM-280193, a platelet aggregation inhibitor
Kaur, Harveen,Harris, Paul W. R.,Little, Peter J.,Brimble, Margaret A.
supporting information, p. 492 - 495 (2015/03/05)
The first total synthesis of YM-280193, a cyclic depsipeptide that inhibits the ADP-induced aggregation of human platelets, is described. The monomer and dipeptide fragments were prepared using conventional chemistry and subsequently assembled by Fmoc-solid-phase peptide synthesis (Fmoc-SPPS). A late-stage novel bis-alkylation-elimination of cysteine on-resin was employed to introduce the unnatural N-methyldehydroalanine moiety. The final step involved execution of a key macrolactamization reaction between the hindered unnatural N,O-dimethylthreonine and ?2-hydroxyleucine residues.