Modulating Oxytocin Activity and Plasma Stability by Disulfide Bond Engineering was written by Muttenthaler, Markus;Andersson, Asa;de Araujo, Aline D.;Dekan, Zoltan;Lewis, Richard J.;Alewood, Paul F.. And the article was included in Journal of Medicinal Chemistry in 2010.Recommanded Product: 156311-83-0 The following contents are mentioned in the article:
Disulfide bond engineering is an important approach to improve the metabolic half-life of cysteine-containing peptides. Eleven analogs of oxytocin were synthesized including disulfide bond replacements by thioether, selenylsulfide, diselenide, and ditelluride bridges, and their stabilities in human plasma and activity at the human oxytocin receptor were assessed. The cystathionine (Ki = 1.5 nM, and EC50 = 32 nM), selenylsulfide (Ki = 0.29/0.72 nM, and EC50 = 2.6/154 nM), diselenide (Ki = 11.8 nM, and EC50 = 18 nM), and ditelluride analogs (Ki = 7.6 nM, and EC50 = 27.3 nM) retained considerable affinity and functional potency as compared to oxytocin (Ki = 0.79 nM, and EC50 = 15 nM), while shortening the disulfide bridge abolished binding and functional activity. The mimetics showed a 1.5-3-fold enhancement of plasma stability as compared to oxytocin (t1/2 = 12 h). By contrast, the all-
((3H-[1,2,3]Triazolo[4,5-b]pyridin-3-yl)oxy)tri(pyrrolidin-1-yl)phosphonium hexafluorophosphate(V) (cas: 156311-83-0) belongs to triazole derivatives. Triazoles exhibit substantial isomerism, depending on the positioning of the nitrogen atoms within the ring. The presence of the three nitrogen atoms in triazole structures afforded opportunities for a plethora of structural modification with the generation of novel therapeutically potential agents, which is different from other heterocyclic compounds.Recommanded Product: 156311-83-0
Referemce:
1,2,3-Triazole – Wikipedia,
Triazoles – an overview | ScienceDirect Topics