5740-47-6Relevant articles and documents
HYDROXAMATE COMPOUNDS AS ANTAGONISTS OF THE ADENOSINE A2A RECEPTOR
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Paragraph 00500; 00549, (2021/01/23)
The present invention relates to compounds of formula I shown below: (I) wherein R1, R2 and R3 are each as defined in the application. The present invention also relates to processes for the preparation of these compounds, to pharmaceutical compositions comprising them, and to their use in the treatment of diseases or conditions in which adenosine A2a receptor activity is implicated, such as, for example, cancer.
Heartleaf houtluynia derivatives and their use in medicine
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Paragraph 0336; 0337, (2018/02/04)
The invention relates to houttuynia cordata derivatives or esters thereof, or an enantiomer or a diastereomer, stereomer, tautomer, hydate, solvate, predrug, or pharmaceutically acceptable salt. In addition, the invention further relates to a preparation method of the houttuynia cordata derivatives, and an application of the houttuynia cordata derivatives in a drug; and the invention further relates to a pharmaceutical composition of the compound, and applications in preparing an antibacterial and anti-virus drug especially used for treating various urinary system diseases, and the advantages are that the water solubility is good, the bioavailability is high, the purity is high, and the toxic and side effects and the stimulation effect due to low purity can be greatly reduced.
Design of a "new motif" with β-amino acids and α-aminoxy acids: Synthesis of hybrid peptides with 12/10-helix
Sharma, Gangavaram V. M.,Manohar, Vennampalli,Dutta, Samit K.,Subash, Velaparthi,Kunwar, Ajit C.
, p. 3689 - 3698 (2008/09/19)
(Figure Presented) Hybrid peptides are prepared from a C-linked carbo-β-amino acid ester (R-β-Caa) and an α-aminoxy acid (R-Ama) derived from S-lactic acid. Extensive NMR (in CDCl3 solution), CD, and MD studies on the tetra- and hexapeptides led to identification of robust 12/10-mixed helices. The dipeptide repeat having an R-β-Caa and an R-Ama thus provides a "new motif" to realize a 12/10-mixed helix, for the first time, in oligomers containing R-Ama. To understand the impact of side chains in the mixed helix formation, R-β-Caa/Ama (with no substitution in Ama) and S-β-hAla/R-Ama oligomers were investigated. NMR studies revealed the existence of 12/10-helices in these hybrid peptides, and the side chains of monomers were found to have a profound influence on their stabilities. These observations imply that the propensity of β-amino acid to prefer a mixed 12/10-helix governs the structural behavior in these peptides. The structural consequences of the lone-pair repulsion between nitrogen and oxygen atoms result in a new and interesting structural motif which behaves like "pseudo" β3,β2-peptides in generating 12/10-mixed helices.