Issue 42, 2023, Issue in Progress
From the journal:

RSC Advances

Affinity- and activity-based probes synthesized from structurally diverse hops-derived xanthohumol flavonoids reveal highly varied protein profiling in Escherichia coli†

Lucas C. Webber,a   Lindsey N. Anderson,a   Ines L. Paraiso,b   Thomas O. Metz, ORCID logo a   Ryan Bradley,cd   Jan F. Stevensb  and  Aaron T. Wright ORCID logo *aef  

* Corresponding authors

a Biological Sciences Division, Pacific Northwest National Laboratory, Richland, Washington 99352, USA
E-mail: a_wright@baylor.edu

b Department of Chemistry, Linus Pauling Institute, Oregon State University, Corvallis, Oregon 97331, USA

c Helfgott Research Institute, National University of Natural Medicine, Portland, Oregon 97201, USA

d Herbert Wertheim School of Public Health and Human Longevity Science, University of California, San Diego, La Jolla, CA 92093, USA

e Department of Biology, Baylor University, Waco, Texas, USA

f Department of Chemistry & Biochemistry, Baylor University, Waco, Texas, USA

Abstract

Xanthohumol, the principle prenylflavonoid found in hops (Humulus lupulus) 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 Escherichia coli, 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.

Graphical abstract: Affinity- and activity-based probes synthesized from structurally diverse hops-derived xanthohumol flavonoids reveal highly varied protein profiling in Escherichia coli

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Article information

DOI
https://doi.org/10.1039/D3RA05296F
Article type
Paper
Submitted
04 Aug 2023
Accepted
18 Sep 2023
First published
11 Oct 2023
This article is Open Access
Creative Commons BY-NC license

RSC Adv., 2023,13, 29324-29331

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Affinity- and activity-based probes synthesized from structurally diverse hops-derived xanthohumol flavonoids reveal highly varied protein profiling in Escherichia coli

L. C. Webber, L. N. Anderson, I. L. Paraiso, T. O. Metz, R. Bradley, J. F. Stevens and A. T. Wright, RSC Adv., 2023, 13, 29324 DOI: 10.1039/D3RA05296F

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