Sensing of citrulline modifications in histone peptides by deep cavitand hosts

Adam D Gill; Briana L Hickey; Siwen Wang; Min Xue; Wenwan Zhong; Richard J Hooley

doi:10.1039/c9cc07002h

Sensing of citrulline modifications in histone peptides by deep cavitand hosts

Chem Commun (Camb). 2019 Oct 31;55(88):13259-13262. doi: 10.1039/c9cc07002h.

Authors

Adam D Gill¹, Briana L Hickey², Siwen Wang³, Min Xue⁴, Wenwan Zhong⁴, Richard J Hooley⁵

Affiliations

¹ Department of Biochemistry and Molecular Biology, University of California-Riverside, Riverside, CA 92521, USA. richard.hooley@ucr.edu.
² Department of Chemistry, University of California-Riverside, Riverside, CA 92521, USA.
³ Environmental Toxicology Program, University of California-Riverside, Riverside, CA 92521, USA.
⁴ Department of Chemistry, University of California-Riverside, Riverside, CA 92521, USA and Environmental Toxicology Program, University of California-Riverside, Riverside, CA 92521, USA.
⁵ Department of Chemistry, University of California-Riverside, Riverside, CA 92521, USA and Department of Biochemistry and Molecular Biology, University of California-Riverside, Riverside, CA 92521, USA. richard.hooley@ucr.edu.

Abstract

Arrayed cavitand:fluorophore sensor complexes can selectively sense small citrulline modifications at arginine residues on post-translationally modified peptides. The sensor can differentiate between different numbers of citrulline modifications, and a simple two-fluorophore, 6-component array can effect cross-reactive discrimination between single modifications in aqueous solution.

Grants and funding

R03 AI139916/AI/NIAID NIH HHS/United States