61274-13-3Relevant articles and documents
Argininamide-type neuropeptide y Y1 receptor antagonists: The nature of: N Ω-carbamoyl substituents determines Y1R binding mode and affinity
Buschmann, Jonas,Keller, Max,Seiler, Theresa,Wifling, David,Bernhardt, Günther
supporting information, p. 274 - 282 (2020/04/17)
The recently resolved crystal structure of the neuropeptide Y Y1 receptor (Y1R), co-crystallized with the high-affinity (pKi: 10.11), argininamide-type Y1R antagonist UR-MK299 (2), revealed that the NΩ-carbamoyl substituent (van der Waals volume: 139 ?3) is deeply buried in the receptor, occupying a hydrophobic pocket. We synthesized and characterized a series of argininamides, structurally related to 2. Y1R affinity decreased with increasing size of the carbamoyl residue (minimal pKi: 5.67). Exceeding a critical size of the substituent (van der Waals volume: 212 ?3), the ligands bound in an inverted mode with the carbamoyl side chain located at the surface of the receptor, as suggested by induced-fit docking and MD simulations.
An efficient procedure for the preparation of carboxamides and peptides using in situ generated N-succinimidyl active esters
Han, Ki-Jong,Kim, Misoo
, p. 370 - 375 (2014/08/05)
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Aerobic amide bond formation with N-hydroxysuccinimide
Yao, Haoyi,Yamamoto, Kana
supporting information; experimental part, p. 1542 - 1545 (2012/09/08)
Breathe easy: Molecular oxygen is one of the most abundant, atom-efficient, and economical oxidants. An aerobic oxidative amide formation from aldehydes and amines is reported. The method uses a catalytic amount of Co(OAc) 2 and N-hydroxysuccinimide as reaction promoters. It is applicable to chiral substrates without loss of their optical purity. Copyright