2480-95-7Relevant academic research and scientific papers
Solid-Phase Synthesis of Substrate-Based Dipeptides and Heterocyclic Pseudo-dipeptides as Potential NO Synthase Inhibitors
Boucher, Jean-Luc,Bouzekrini, Amine,Hamzé, Abdallah,Hernandez, Jean-Fran?ois,Lajoix, Anne-Dominique,Leroy, Jérémy,Martinez, Jean,Mauchauffée, Elodie,Mezghenna, Karima,Ramassamy, Booma,Tintillier, Thibault,Touati-Jallabe, Youness,Verna, Claudia
, (2020)
More than 160 arginine analogues modified on the C-terminus via either an amide bond or a heterocyclic moiety (1,2,4-oxadiazole, 1,3,4-oxadiazole and 1,2,4-triazole) were prepared as potential inhibitors of NO synthases (NOS). A methodology involving formation of a thiocitrulline intermediate linked through its side-chain on a solid support followed by modification of its carboxylate group was developed. Finally, the side-chain thiourea group was either let unchanged, S-alkylated (Me, Et) or guanidinylated (Me, Et) to yield respectively after TFA treatment the corresponding thiocitrulline, S-Me/Et-isothiocitrulline and N-Me/Et-arginine substrate analogues. They all were tested against three recombinant NOS isoforms. Several compounds containing a S-Et- or a S-Me-Itc moiety and mainly belonging to both the dipeptide-like and 1,2,4-oxadiazole series were shown to inhibit nNOS and iNOS with IC50 in the 1–50 μM range. Spectral studies confirmed that these new compounds interacted at the heme active site. The more active compounds were found to inhibit intra-cellular iNOS expressed in RAW264.7 and INS-1 cells with similar efficiency than the reference compounds L-NIL and SEIT.
A synthetic approach to 5/5/6-polycyclic tetramate macrolactams of the discodermide type
Bodenschatz, Kevin,St?ckl, Julia,Winterer, Markus,Schobert, Rainer
, (2021/05/31)
A flexible synthetic route to the 16-membered tetramate-embedding macrocyclic scaffold present in various polycyclic tetramate macrolactams (PTMs) was developed which differs from the seminal synthesis of ikarugamycin by Boeckman Jr. in protecting groups and the order of connections. We also devised a short approach to various stereoisomers of the 5/5/6-tricarbocyclic motif found in discodermide and other PTMs, starting from the Weiss’ diketone.
Caffeic acid derivatives: A new type of influenza neuraminidase inhibitors
Xie, Yuanchao,Huang, Bing,Yu, Kexiang,Shi, Fangyuan,Liu, Tianqi,Xu, Wenfang
supporting information, p. 3556 - 3560 (2013/07/04)
Recently, many natural products, especially some plant-derived polyphenols have been found to exert antiviral effects against influenza virus and show inhibitory activities on neuraminidases (NAs). In our research, we took caffeic acid which contained two phenolic hydroxyl groups as the basic fragment to build a small compound library with various structures. The enzyme inhibition result indicated that some compounds exhibited moderate activities against NA and compound 15d was the best with IC50 = 7.2 μM and 8.5 μM against N2 and N1 NAs, respectively. The 3,4-dihydroxyphenyl group from caffeic acid was important for the activity according to the docking analysis. Besides, compound 15d was found to be a non-competitive inhibitor with Ki = 11.5 ± 0.25 μM by the kinetic study and also presented anti-influenza virus activity in chicken embryo fibroblast cells. It seemed promising to discover more potent NA inhibitors from caffeic acid derivatives to cope with influenza virus.
Inhibitors of N α-acetyl-l-ornithine deacetylase: Synthesis, characterization and analysis of their inhibitory potency
Hlavacek,Picha,Vanek,Jiracek,Slaninova,Fucik,Budesinsky,Gilner,Holz
experimental part, p. 1155 - 1164 (2010/08/06)
A series of N α-acyl (alkyl)- and N α- alkoxycarbonyl-derivatives of l- and d-ornithine were prepared, characterized, and analyzed for their potency toward the bacterial enzyme N α-acetyl-l-ornithine deacetylase (ArgE). Ar
