{"id":2365,"date":"2019-08-13T13:40:00","date_gmt":"2019-08-13T12:40:00","guid":{"rendered":"https:\/\/sites.dundee.ac.uk\/alessio-ciulli\/?p=2365"},"modified":"2026-01-26T16:28:04","modified_gmt":"2026-01-26T16:28:04","slug":"our-review-on-bispecific-small-molecules-that-bring-proteins-together-is-published-in-current-opinion-in-chemical-biology","status":"publish","type":"post","link":"https:\/\/sites.dundee.ac.uk\/alessio-ciulli\/2019\/08\/13\/our-review-on-bispecific-small-molecules-that-bring-proteins-together-is-published-in-current-opinion-in-chemical-biology\/","title":{"rendered":"Our review on bispecific small molecules that bring proteins together is published in Current Opinion in Chemical Biology"},"content":{"rendered":"

Well done Chiara!<\/p>\n

Read the full article<\/a>.<\/p>\n

Authors<\/strong>: Chiara Maniaci and Alessio Ciulli*<\/p>\n

Title<\/strong>:\u00a0Bifunctional chemical probes inducing protein-protein interactions.<\/p>\n

Abstract<\/strong><\/h2>\n

Inducing biomolecular interactions with synthetic molecules to impact biological function is a concept of enormous appeal. Recent years have seen a resurgence of interest in designing bispecific molecules that serve as bridging agents to bring proteins together. Pioneering structural and biophysical investigation of ternary complexes formed by mono-functional and bifunctional ligands highlights that proximity-induced stabilization or de novo formation of protein\u2013protein interactions is a common feature of their molecular recognition. In this review, we illustrate these concepts and advances with representative case studies, and highlight progress over the past three years, with particular focus on recruitment to E3 ubiquitin ligases by \u2018molecular glues\u2019 and chimeric dimerizers (PROTACs) for targeted protein degradation. This approach promises to significantly expand the range of tractable targets for chemical biology and therapeutic intervention.<\/p>\n