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Relevant academic research and scientific papers

Macrocyclic amines as catalysts of the hydrolysis of the triphosphate bridge of the mRNA 5′-cap structure

The reactions of a 5′-cap model compound P 1-(7-methylguanosine) P3-guanosine 5′,5′-triphosphate, m7GpppG, were studied in the presence of three different macrocyclic amines (2-4) under neutral conditions. The only products observed in the absence of the macrocycles resulted from the base-catalysed imidazole ring-opening and the acid-catalysed cleavage of the N7-methylguanosine base, whereas in the presence of these catalysts hydrolysis of the triphosphate bridge predominated. The latter reaction yielded guanosine 5′-monophosphate, guanosine 5′-diphosphate, 7-methylguanosine 5′-monophosphate and 7-methylguanosine 5′-diphosphate as the initial products, indicating that both of the phosphoric anhydride bonds were cleaved. The overall catalytic activity of all three macrocycles was comparable. The hydrolysis to guanosine 5′-diphosphate and 7-methylguanosine 5′-monophosphate was slightly more favoured than the cleavage to yield guanosine 5′-monophosphate and 7-methylguanosine diphosphate. All the macrocycles also enhanced the subsequent hydrolysis of the nucleoside diphosphates, 2 being more efficient than 3 and 4.

The Cu2+-promoted cleavage of mRNA 5'-cap analogs: A kinetic study with p1(7-methylguanosin-5'-yl) p3-(nucleosid-5'-yl) triphospates and p1- (7-methylguanosin-5'-yl) p4-(guanosin-5'-yl) tetraphosphate

A kinetic study on the cleavage of a number of mRNA 5'-cap analogs, m7GpppN and m7GppppG, with Cu2+ aquo ion has been performed. Time- dependent product distributions at various pH and metal ion concentrations have been determined by capillary zone electrophoresis, and these data have been used to calculate the rate constants for various parallel reactions of the breakdown of the cap analogs.