Site-Selective Protein Modification via Peptide-Directed Proximity Catalysis
Year: 2025
Type: article
Abstract: High Resolution Image Download MS PowerPoint Slide Proximity catalysis exploits ligand binding for localized, catalytic protein modification. In this work, we introduce catalyst-functionalized peptides as versatile ligands for this approach. Through the functionalization of target-binding peptides with pyridinium oxime catalysts, we show that model proteins can be site-selectively modified with a variety of N -acyl- N -alkylsulfonamide reagents to introduce common functionalities, including fluorophores and affinity handles to the protein surface. Critically, we show that simple changes to the peptide-catalyst structure, moving the pyridinium oxime from the N- to C-terminus, alter the site of modification. This opens up possibilities to develop peptide libraries for a particular target protein and subsequently tuning the modification site for a given application.
Source: ACS Omega
Institution: University of York
Language: English
Subfield: Organic Chemistry
Field: Chemistry
Domain: Physical Sciences
Open Access status: gold
Estimated APC paid: $1,935
Awards: Technologies for the Future, Probing the dynamics, orientation and conformation of lipopolysaccharide in bacterial membranes through bioorthogonal chemistry and single-molecule bi, Improving in vitro tissue models through bioactive materials, Photonic hyperspectral no-label spotter (PHENOSPOT), Core Capability - University of York, G7369490160, Improving in vitro tissue models through bioactive materials
OpenAlex ID: W4417452467