Structural analysis of the inhibitory effects of polyphenols, (+)‐hopeaphenol and (−)‐isohopeaphenol, on human SIRT1
Human sirtuin 1 (hSIRT1) is a NAD+‐dependent deacetylase that regulates several cellular processes. Unlike resveratrol, natural polymeric phenolic compounds isolated from Vitaceae are mostly hSIRT1 inhibitors. The resveratrol tetramer, (+)‐hopeaphenol ((+)‐HP), and its geometric isomer, (−)‐isohopea...
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| Veröffentlicht in: | BioFactors (Oxford) 2019-03, Vol.45 (2), p.253-258 |
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| container_title | BioFactors (Oxford) |
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| creator | Loisruangsin, Arthorn Hikita, Kiyomi Seto, Norikazu Niwa, Masatake Takaya, Yoshiaki Kaneda, Norio |
| description | Human sirtuin 1 (hSIRT1) is a NAD+‐dependent deacetylase that regulates several cellular processes. Unlike resveratrol, natural polymeric phenolic compounds isolated from Vitaceae are mostly hSIRT1 inhibitors. The resveratrol tetramer, (+)‐hopeaphenol ((+)‐HP), and its geometric isomer, (−)‐isohopeaphenol ((−)‐iHP), were tested for inhibitory effects on purified hSIRT1 using a fluorescent derivative of peptide substrate p53‐AMC (Fluor de Lys) and a cofactor NAD+. The Lineweaver–Burk plots indicated that both (+)‐HP and (−)‐iHP were competitive inhibitors against NAD+. Computer‐assisted modeling of the binding of these molecules with hSIRT1 protein provided the most feasible conformation of the enzyme–inhibitor complex. © 2018 BioFactors, 45(2):253–258, 2019 |
| doi_str_mv | 10.1002/biof.1479 |
| format | Article |
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Unlike resveratrol, natural polymeric phenolic compounds isolated from Vitaceae are mostly hSIRT1 inhibitors. The resveratrol tetramer, (+)‐hopeaphenol ((+)‐HP), and its geometric isomer, (−)‐isohopeaphenol ((−)‐iHP), were tested for inhibitory effects on purified hSIRT1 using a fluorescent derivative of peptide substrate p53‐AMC (Fluor de Lys) and a cofactor NAD+. The Lineweaver–Burk plots indicated that both (+)‐HP and (−)‐iHP were competitive inhibitors against NAD+. Computer‐assisted modeling of the binding of these molecules with hSIRT1 protein provided the most feasible conformation of the enzyme–inhibitor complex. © 2018 BioFactors, 45(2):253–258, 2019</abstract><cop>Hoboken, USA</cop><pub>John Wiley & Sons, Inc</pub><pmid>30537158</pmid><doi>10.1002/biof.1479</doi><tpages>6</tpages><orcidid>https://orcid.org/0000-0001-7796-7074</orcidid><orcidid>https://orcid.org/0000-0003-0464-2070</orcidid></addata></record> |
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| subjects | (+)‐hopeaphenol (−)‐isohopeaphenol human SIRT1 Humans MD simulation molecular docking Phenols - chemistry Phenols - pharmacology Polyphenols - chemistry Polyphenols - pharmacology Protein Binding Resveratrol - chemistry Resveratrol - pharmacology resveratrol tetramer Sirtuin 1 - antagonists & inhibitors Sirtuin 1 - chemistry Sirtuin 1 - metabolism Stilbenes - chemistry Stilbenes - pharmacology |
| title | Structural analysis of the inhibitory effects of polyphenols, (+)‐hopeaphenol and (−)‐isohopeaphenol, on human SIRT1 |
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