Control of Protein-Protein Interactions: Structure-Based Discovery of Low Molecular Weight Inhibitors of the Interactions between Pin1 WW Domain and Phosphopeptides was written by Smet, Caroline;Duckert, Jean-Frederic;Wieruszeski, Jean-Michel;Landrieu, Isabelle;Buee, Luc;Lippens, Guy;Deprez, Benoit. And the article was included in Journal of Medicinal Chemistry in 2005.SDS of cas: 86069-86-5 The following contents are mentioned in the article:
Interactions involving phosphorylated Ser/Thr-Pro motifs in proteins play a key role in numerous regulatory processes in the cell. Here, we investigate potential ligands of the WW binding domain of Pin1 in order to inhibit protein-protein interactions between Pin1 and phosphopeptides. Our structure-based strategy implies the synthesis of analogs of the Ac-Thr(PO3H2)-Pro-NH2 dipeptide and relies on high resolution NMR spectroscopy to accurately measure the affinity constants even in the high micromolar range. This study involved multiple reactions and reactants, such as (S)-1-(((9H-Fluoren-9-yl)methoxy)carbonyl)piperidine-2-carboxylic acid (cas: 86069-86-5SDS of cas: 86069-86-5).
(S)-1-(((9H-Fluoren-9-yl)methoxy)carbonyl)piperidine-2-carboxylic acid (cas: 86069-86-5) belongs to piperidine derivatives. Piperidine is a metabolite of cadaverine, a polyamine found in the human intestine. Industrially, piperidine is produced by the hydrogenation of pyridine, usually over a molybdenum disulfide catalyst. Pyridine can also be reduced to piperidine via a modified Birch reduction using sodium in ethanol.SDS of cas: 86069-86-5
Referemce:
Piperidine – Wikipedia,
Piperidine | C5H11N – PubChem