Interaction of human serum albumin and its clinically relevant modification with oligoribonucleotides

RNA hydrolysis in the presence of HSA proceeds via 2′,3′-cyclophosphate intermediates. Nonenzymatic glycation of HSA decreases protein-mediated oligoribonucleotide cleavage with no influence on the cleavage specificity. Human serum albumin (HSA) was shown to mediate oligoribonucleotide cleavage. Non...

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Veröffentlicht in:Bioorganic & medicinal chemistry 2008-08, Vol.18 (16), p.4511-4514
Hauptverfasser: Gerasimova, Yuliya V., Erchenko, Irina A., Shakirov, Makhmut M., Godovikova, Tatyana S.
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Sprache:eng
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Zusammenfassung:RNA hydrolysis in the presence of HSA proceeds via 2′,3′-cyclophosphate intermediates. Nonenzymatic glycation of HSA decreases protein-mediated oligoribonucleotide cleavage with no influence on the cleavage specificity. Human serum albumin (HSA) was shown to mediate oligoribonucleotide cleavage. Nonenzymatic glycation of HSA decreased the ribonuclease-like activity of the protein. According to 31P NMR data, both native and glycated albumins induced hydrolysis of RNA molecule through 2′,3′-cyclophosphate intermediates. A feasible mechanism of RNA hydrolysis by native albumin and its clinically relevant modification was discussed.
ISSN:0960-894X
0968-0896
1464-3405
1464-3391
DOI:10.1016/j.bmcl.2008.07.060