TitleAffinity- and activity-based probes synthesized from structurally diverse hops-derived xanthohumol flavonoids reveal highly varied protein profiling in .
Publication TypeJournal Article
Year of Publication2023
AuthorsWebber LC, Anderson LN, Paraiso IL, Metz TO, Bradley R, Stevens JF, Wright AT
JournalRSC Adv
Date Published2023 Oct 04

Xanthohumol, the principle prenylflavonoid found in hops () and a reported anti-inflammatory agent, has great potential for pharmaceutical interventions related to inflammatory disorders in the gut. A suite of probes was prepared from xanthohumol and its structural isomer isoxanthohumol to enable profiling of both protein affinity binding and catalytic enzyme reactivity. The regiochemistry of the reactive group on the probes was altered to reveal how probe structure dictates protein labeling, and which probes best emulate the natural flavonoids. Affinity- and activity-based probes were applied to , and protein labeling was measured by chemoproteomics. Structurally dependent activity-based probe protein labeling demonstrates how subtle alterations in flavonoid structure and probe reactive groups can result in considerably different protein interactions. This work lays the groundwork to expand upon unexplored cellular activities related to xanthohumol interactions, metabolism, and anti-inflammatory mechanisms.

Alternate JournalRSC Adv
PubMed ID37829707
PubMed Central IDPMC10565736
Grant ListR01 AT010271 / AT / NCCIH NIH HHS / United States
R90 AT008924 / AT / NCCIH NIH HHS / United States