Basel: Crosslinkers as tools for protein di- or trimerisation, diagnostics and therapy

Licensing opportunity

Recent studies have shown great promise for small molecules that specifically bring two or more proteins together, prompting enhanced or novel biological effects. However, until now, the demonstration of acceptable performances of current S-CROSS molecules (protein complexes detected via selective covalent cross-linking) has been possible only in vitro.

New research by scientists at the University of Basel relates to homo- or hetero-functional molecules containing the substrate of one or multiple protein tags, for labelling bio-molecules like lipids, proteins, DNA, RNA or carbohydrates. Tag substrates, or labels, are covalently connected via a fluorolinker, or rapalog, which increases the rate of penetration of substrates into cells by means of trans-membrane diffusion and or/preventing the exit from the cell body.

This new technique enables the in vivo induction of protein assemblies, and its modular chemical design supports inducible protein multimerisation. It also allows for covalent binding of protein partners with potential new biological effects and high-efficiency protein cross-linker internalisation and bioavailability. It is a cost effective, versatile and short synthesis of chemical substrates, with open access to protein trimerisation assays.

Inducible protein multimerisation or translocation in living organisms is likely to be of utility in research, diagnostics, analytics and therapeutic applications.