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 |
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Hauptverfasser: | , , , |
Format: | Artikel |
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. |
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ISSN: | 0960-894X 0968-0896 1464-3405 1464-3391 |
DOI: | 10.1016/j.bmcl.2008.07.060 |