103517-57-3Relevant articles and documents
Structure-based design of potent, amidine-derived inhibitors of factor Xa: Evaluation of selectivity, anticoagulant activity, and antithrombotic activity
Wiley, Michael R.,Weir, Leonard C.,Briggs, Steven,Bryan, Nancy A.,Buben, John,Campbell, Charles,Chirgadze, Nickolay Y.,Conrad, Richard C.,Craft, Trelia J.,Ficorilli, James V.,Franciskovich, Jeffry B.,Froelich, Larry L.,Gifford-Moore, Donetta S.,Goodson Jr., Theodore,Herron, David K.,Klimkowski, Valentine J.,Kurz, Kenneth D.,Kyle, Jeffery A.,Masters, John J.,Ratz, Andrew M.,Milot, Guy,Shuman, Robert T.,Smith, Tommy,Smith, Gerald F.,Tebbe, Ann Louise,Tinsley, Jennifer M.,Towner, Richard D.,Wilson, Alexander,Yee, Ying K
, p. 883 - 899 (2000)
To enhance the potency of 1,2-dibenzamidobenzene-derived inhibitors of factor Xa (fXa), an amidine substituent was incorporated on one of the benzoyl side chains to interact with Asp189 in the S1 specificity pocket. Lead molecule I was docked into the act
Buchwald-Hartwig amination of aryl esters and chlorides catalyzed by the dianisole-decorated Pd-NHC complex
Zheng, Di-Zhong,Xiong, Hong-Gang,Song, A-Xiang,Yao, Hua-Gang,Xu, Chang
supporting information, p. 2096 - 2101 (2022/04/01)
A modular and generic method for the Buchwald-Hartwig amination reactions of relatively unreactive aryl esters as acyl electrophiles and aryl chlorides as aryl electrophiles has been developed, leading to the efficient synthesis of amides/amines under air conditions and with low catalyst loadings. The success of this catalytic protocol is mainly attributed to the modification of the Pd-IPr skeleton with sterically hindered and electron-donating anisole groups. This method also features good functional group tolerance and excellent chemoselectivities. In summary, the results presented herein suggest the possibility of developing a versatile and general protocol for diverse electrophiles to undergo the Buchwald-Hartwig amination reactions, avoiding too much consideration of the reaction conditions for the substrate-dependent C-N bond formations.
Folding Patterns in a Family of Oligoamide Foldamers
Kortelainen, Minna,Suhonen, Aku,Hamza, Andrea,Pápai, Imre,Nauha, Elisa,Yliniemel?-Sipari, Sanna,Nissinen, Maija,Pihko, Petri M.
supporting information, p. 9493 - 9504 (2015/06/30)
A series of small, unsymmetrical pyridine-2,6-dicarboxylamide oligoamide foldamers with varying lengths and substituents at the end groups were synthetized to study their conformational properties and folding patterns. The @-type folding pattern resembled the oxyanion-hole motifs of enzymes, but several alternative folding patterns could also be characterized. Computational studies revealed several alternative conformers of nearly equal stability. These folding patterns differed from each other in their intramolecular hydrogen-bonding patterns and aryl-aryl interactions. In the solid state, the foldamers adopted either the globular @-type fold or the more extended S-type conformers, which were very similar to those foldamers obtained computationally. In some cases, the same foldamer molecule could even crystallize into two different folding patterns, thus confirming that the different folding patterns are very close in energy in spite of their completely different shapes. Finally, the best match for the observed NOE interactions in the liquid state was a conformation that matched the computationally characterized helix-type fold. Erase and refold: Like peptides, oligoamide foldamers fold into a number of different conformers that are very close in energy (see picture, stability energies in kcal mol-1 given in parentheses). By using a combination of computational, single-crystal X-ray diffraction, and NMR spectroscopic studies, these folding patterns have been identified and characterized for a family of seven different foldamers with varying substituents.
