Publication

N-terminal protein recognition by supramolecular synthons

Wren, Colin
Thumbnail Image
Files
2024WrenResearchMasters.pdf
Adobe PDF, 3.68 MB
Identifiers
https://hdl.handle.net/10379/18757
 https://doi.org/10.13025/29551
Publication Date
2025-03-28
Keywords
biomolecular recognition, WPCTX, Biological and Chemical Sciences, Chemistry
Type
master thesis
Downloads
Show all metadata
Citation
Abstract
This research investigate the biomolecular recognition capabilities of WPCTX, an anionic phosphocavitand. Cocrystallization trials of WPCTX and two different model proteins were performed. X-ray crystallography was used to elucidate the structures of the resulting crystals. NMR spectroscopy was used to characterize the protein – macrocycle interactions in solution. WPCTX bound arginine residues in lysozyme in a trigonal cocrystal form. Three related cocrystal forms of RSL – WPCTX revealed N-terminal binding across a variety of crystallization conditions. MK-RSL, a mutant of RSL containing an extended N-terminus with a Met-Lys motif showed further N-terminal binding with WPCTX. The macrocycle in RSL and MK-RSL cocrystals, formed clusters that mediated protein assembly. These results identify a synthetic ligand capable of N-terminal recognition as well as self-assembly (cluster formation) furthering our knowledge as to how supramolecular synthons may aid protein assembly.
Funder
Publisher
University of Galway
Publisher DOI
Rights
Attribution-NonCommercial-NoDerivatives 4.0 International
cbn
Collections
University of Galway Theses (Research Masters Theses)