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Results for “GLUCOSAMINE”

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Carboxy derivatized glucosamine is a potent inhibitor of matrix metalloproteinase-9 in HT1080 cells.

Experimental evidences have confirmed that matrix metalloproteinases (MMPs) play a fundamental role in a wide variety of pathologic conditions and recent advances in medicinal chemistry approach to the design of MMP inhibitors with desired structural and functional properties. Among MMPs, MMP-9 has demonstrated to play a major role in the establishment of metastases and it is substantially increased in the majority of malignant tumors. Inhibition of MMP-9 is thought to have a therapeutic benefit to cancer. Results of this study present a novel synthetic MMP-9 inhibitor that downregulates MMP-9 expression level in HT1080, human fibrosarcoma cells.

Cell Line, Tumor↗

Artificial N-functionalized UDP-glucosamine analogues as modified substrates for N-acetylglucosaminyl transferases.

Analogues of UDP-GlcNAc modified at the 2-acetamido group of the GlcNAc moiety were prepared in order to study their role in the mechanism of N-acetylglucosaminyl transferase mediated glycosylation reactions. The structural analogues with N-formyl-, N-propionyl-, N-butyryl- and N-isobutyryl-groups were synthesized, utilizing the morpholidate coupling method starting from d-glucosaminyl-1-phosphate after selective N-acylation of its amino group with the appropriate N-acyloxysuccinimide esters as well as a chlorinated formylformiate.

Glucosamine↗

Synthesis of new sugar amino acid derivatives of D-glucosamine.

The synthesis of several new sugar amino acid derivatives of 2-acetamido-2-deoxy-D-glucose, bearing a C-glycosyl functionality as building blocks for the design and synthesis of natural glycoconjugates mimetics, is described. These compounds were prepared from the readily accessible per-benzylated amino C-allyl glucopyranosyl compounds, with TMSOTf/Ac(2)O-mediated selective acetolysis of the 6-O-benzyl group as the key step.

Acetylglucosamine↗