Cyclic peptide-based potent and selective SIRT1/2 dual inhibitors harboring NÎµ-thioacetyl-lysine

Article ID	Journal	Published Year	Pages	File Type
5155554	Bioorganic & Medicinal Chemistry Letters	2016	6 Pages	PDF

Abstract

N-terminus-to-side chain cyclic tripeptides (4, 5, 12) harboring the catalytic mechanism-based SIRT1/2/3 inhibitory warhead NÎµ-thioacetyl-lysine at their central positions were found to exhibit strong and selective (versus SIRT3/5/6) dual SIRT1/2 inhibition.125

Keywords

DMF 2-(1H-benzotriazole-1-yl)-1,1,3,3-tetramethylaminium hexafluorophosphate β-NAD+DCM 4-methylbenzhydrylamine IC50 TFA RP-HPLC MBHA HRMS sirtuin N-methylmorpholine NMM SPPS HBTU N,N-dimethylformamide β-nicotinamide adenine dinucleotide Trifluoroacetic acid Inhibitor Dichloromethane Solid phase peptide synthesis high-resolution mass spectrometry Cyclic peptide reversed-phase high performance liquid chromatography