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• W2111862114 abstract "Abstract Suramin is a symmetric polyanionic naphthylurea originally used for the treatment of trypanosomiasis and onchocerciasis. Suramin and diverse analogues exhibit a broad range of biological actions in vitro and in vivo, including, among others, antiproliferative and antiviral activity. Suramin derivatives usually target purinergic binding sites. Class III histone deacetylases (sirtuins) are amidohydrolases that require nicotinamide adenine dinucleotide (NAD + ) as a cofactor for their catalytic mechanism . Deacetylation of the target proteins leads to a change in conformation and alters the activity of the proteins in question. Suramin was reported to inhibit human sirtuin 1 (SIRT1). We tested a diverse set of suramin analogues to elucidate the inhibition of the NAD + ‐dependent histone deacetylases SIRT1 and SIRT2 and discovered selective inhibitors of human sirtuins with potency in the two‐digit nanomolar range. In addition, the structural requirements for the binding of suramin derivatives to sirtuins were investigated by molecular docking. The recently published X‐ray crystal structure of human SIRT5 in complex with suramin and the human SIRT2 structure were used to analyze the interaction mode of the novel suramin derivatives." @default.
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• W2111862114 date "2007-09-26" @default.
• W2111862114 modified "2023-10-17" @default.
• W2111862114 title "Structure–Activity Studies on Suramin Analogues as Inhibitors of NAD+-Dependent Histone Deacetylases (Sirtuins)" @default.
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• W2111862114 doi "https://doi.org/10.1002/cmdc.200700003" @default.
• W2111862114 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17628866" @default.
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