5241-71-4Relevant articles and documents
Method for preparing aspartylcyclohexyla laninamide
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Page column 6-7, (2008/06/13)
Disclosure is a method for preparing α-aspartyl-β-cyclohexylalaninamide, comprising carrying out a first step of amide formation of an α-aspartyl phenylamine ester of general formula (II) wherein: R is a C1-C4alkyl radical, and then
Protected-mode Synthesis of N-Linked Glycopeptides: Single-step Preparation of Building Blocks as Peracetyl Glycosylated NαFmoc Asparagine OPfp Esters
Christiansen-Brams, Ida,Meldal, Morten,Bock, Klaus
, p. 1461 - 1472 (2007/10/02)
The preparation of Nα-(fluoren-9-ylmethoxycarbonyl)asparagine pentafluorophenyl esters (Nα-Fmoc-Asn-OPfp) glycosylated with per-O-acetylated β-D-glucose, N-acetyl-β-D-glucosamine, β-D-mannose, 4-O-β-D-glucopyranosyl-β-D-glucose (cellobiose), 4-O-β-D-galactopyranosyl-β-D-glucose (lactose) and 4-O-α-D-glucopyranosyl-β-D-glucose (maltose) is described.The per-O-acetylated glycosylamines were treated selectively with the key compound Nα-Fmoc-Asp(Cl)-OPfp 2, to give, in a single step, the glycosylated building blocks.The acid chloride 2 was prepared in a quantitative one-pot reaction from commercially available Nα-Fmoc-Asp(OBut)-OPfp 1.The acid stability of the N-glycosidic linkage was investigated.The building block 7, containing a maltose moiety, was used in the synthesis of a glycosylated D-Ala1 Peptide-T amide analogue 14.CD spectra were recorded in 85 percent TFE.All compounds were fully characterized by (1)H and (13)C NMR spectroscopy.
PAPAIN-CATALYZED FRAGMENT SYNTHESIS OF PROTECTED CHOLECYSTOKININ DERIVATIVES
Cerovsky, Vaclav,Pirkova, Jana,Majer, Pavel,Slaninova, Jirina,Hlavacek, Jan
, p. 1873 - 1882 (2007/10/02)
Sodium salts of methyl esters of N-tert-butyloxycarbonyl-β-tert-butylaspartyl-O4-sulfotyrosine (II) or N-tert-butyloxycarbonyl-O4-sulfotyrosine (III) were condensed with amino components derived from peptide amides IVb-IVe and IVg (simulating the carboxy-terminal part of cholecystokinin) under catalysis with papain.Rates and yields of conversion of these peptides to the corresponding derivatives Ib-If were compared with the results reported previously for analogous papain-catalyzed fragment synthesis of the protected carboxy-terminal octapeptide of cholecystokinin Ia.In the condensation reactions with the individual amino components quantitative changes were observed in the ability of papain to catalyze the peptide bond synthesis which appeared as differences in the maximum yield (and the time required for achieving it) of the condensation reaction, monitored by HLPC.The observed differences are related not only with the distance of the amino acid substitution from the P'1 subsite in the given amino component but also with the side-chain structure of the substituting amino acid.