Work

Long-lived azobispyrazole stapled peptides for light-activated inhibition of protein–protein interactions

Year: 2026

Type: article

Abstract: (0.5-year half-life) and were tolerant to biological assay conditions. Our work expands the repertoire of photoswitches designed for peptide stapling and demonstrates the ability of azobispyrazole-stapled peptides to modulate protein-protein interactions in a system where binding is controlled exclusively by light, independent of thermal relaxation, over a timescale of several weeks.

Source: Chemical Science

DOI: 10.1039/d6sc06137k

Authors: Sinead McCann, Davia Prischich, Kira Scobel, Dennis J. Worm, Aditya R. Thawani, Marie Mori, Yaw Sing Tan, Anna Barnard, Matthew J. Fuchter

Institutions: Imperial College London, University of Oxford, Agency for Science, Technology and Research, Bioinformatics Institute

Language: English

Topic: Chemical Synthesis and Analysis

Subfield: Organic Chemistry

Field: Chemistry

Domain: Physical Sciences

Open Access status: diamond

Funders: Wellcome Trust, Imperial College London, Agency for Science, Technology and Research, Innovation and Technology Commission, Hong Kong Government, Engineering and Physical Sciences Research Council, Biomedical Research Council

Awards: Targeting Protein-Protein Interactions in Salmonella Persisters: An Innovative Approach to Tackling Recurrent Infections, Targeting Protein-Protein Interactions in Salmonella Persisters: An Innovative Approach to Tackling Recurrent Infections, FUNCTION THROUGH CHIRALITY IN ORGANIC ELECTRONIC MATERIALS AND DEVICES

OpenAlex ID: W7225091302

FWCI:

Cites: 4

Cited by:

Related to: 10