Two analogues of lysine-vasopressin in which the lysine side chain was modified by the attachment of glucuronic acid through the amide bond were synthesized and their pharmacological properties evaluated. In comparison to arginine-vasopressin used as a standard, both analogues were found to exhibit low activity in vasopressor test, moderate activity in antidiuretic test, and comparable activity in uterotonic test.
The carbohydrate moieties, linked to mistletoe lectin 1 (ML-1) are characterized by enzymatic digestion of the individual A and B chains (MLA and MLB), HPLC separation of the (glyco)peptide digests and their sequence and mass spectrometric analysis. All carbohydrate chains are linked via Asn residues to the MLA protein molecule. A xylomannose-type oligosaccharide (1) structure (Man3Xyl1Fuc1GlcNac2) is attached to the Asn112 residue of the A chain. Three different glycosylation sites are identified for the B chain: oligosaccharide II (Man6GlcNac2) is found to be linked to Asn96 as well as Asn136 residues. In homologous mistletoe lectins, isolated from different harvest batches, oligosaccharide III (Man5GlcNac2) is attached to Asn136 instead of oligosaccharide II**.
A mild three-dimensional orthogonal protection scheme, based on Nps/Fmoc-groups for a-amino, benzyl residues for hydroxyl and carboxyl protection and 2-chlorotrityl esters as anchoring linkage proved to be a new effective approach for the synthesis of glycopeptides. The oligosaccharide moiety of the nephritogenoside glycopeptide is conveniently assembled via phenyl thioglycosides as glycosyl acceptors and phenyl thioglycosyl sulfoxides as donors, readily accessible from the thioglycosides by oxidation with m-chloroperbenzoic acid.
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.