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Oxytocin Analogues with O-Glycosylated Serine and Threonine in Position 4

Marcinkowska A., Borovičková L., Slaninová J., Grzonka Z.

Polish Journal of Chemistry

2007

Vol. 81, nr 7

1335-1344

Oxytocin structure was modified in position 4 using glycoamino acids. Procedure for transformation of Fmoc-protected serine and threonine derivatives into appropriate O-glycosylated precursors suitable for solid phase peptide synthesis (SPPS) was worked out. The alfa- and beta-O-glycosides were synthesized from Fmoc-serine and Fmoc-threonine allyl esters and appropriate glycosyl bromide using Hanessian's modification of the Koenigs-Knorr reaction. These N alfa-Fmoc-protected glycoamino acids were used in the synthesis of glycopeptides. Eight analogues of oxytocin were prepared. The obtained glycopeptides were tested for their rat uterotonic in vitro, pressor and antidiuretic activities and for their affinity to human oxytocin receptor. Moreover their stability towards alfa-chymotrypsin cleavage was studied.

Lysine-Vasopressin Analogues with Glycoconjugates in Position 8

Marcinkowska A., Borovickova L., Slaninova J., Grzonka Z.

Polish Journal of Chemistry

2006

Vol. 80, nr 5

759-766

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.

Total Synthesis of the Nephritogenoside Glycopeptide

Zhang H., Wang Y., Thurmer R., Al-Qawasmeh R., Voelter W.

Polish Journal of Chemistry

1999

vol. 73 nr 1

101-115

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.

Carbohydrate Chains and Their Binding Sites in Mistletoe Lectin I

Stoeva S., Maier T., Soler M., Voelter W.

Polish Journal of Chemistry

1999

vol. 73 nr 1

125-133

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**.