Synthesis and characterization of a SIRT6 open tubular column: predicting deacetylation activity using frontal chromatography.

ABSTRACT: SIRT6 is a histone deacetylase that has been proposed as a potential therapeutic target for metabolic disorders and the prevention of age-associated diseases. Thus the identification of compounds that modulate SIRT6 activity could be of great therapeutic importance. We have previously reported on the identification of quercetin and vitexin as SIRT6 inhibitors, using SIRT6-coated magnetic beads. In this study, we have immobilized SIRT6 onto the surface of an open tubular capillary and characterized the quercetin binding site using frontal displacement chromatography. Structurally related flavonoids were tested for their activity on SIRT6, including apigenin, naringenin, luteolin, and kaempferol. In addition to obtaining their binding activity using frontal affinity chromatographic technique

SUBMITTER: Singh N 

PROVIDER: S-EPMC4167792 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature