A further step towards light-controlled drugs

Schematic of the protein-protein interaction. Image: IBEC
Schematic of the protein-protein interaction. Image: IBEC
Research
(22/01/2015)

Last year, a group of scientists from the Insititute for Bioengineering of Catalonia (IBEC), the Institute for Research in Biomedicine (IRB Barcelona) and the University of Barcelona (UB) announced that they had achieved photo-switchable, or light-regulated, molecules to control protein-protein interactions in a remote and non-invasive manner. The discovery signified a major step towards the development of targeted, light-controlled drugs, whose effects would be limited to a specific area and time, reducing side effects.

Schematic of the protein-protein interaction. Image: IBEC
Schematic of the protein-protein interaction. Image: IBEC
Research
22/01/2015

Last year, a group of scientists from the Insititute for Bioengineering of Catalonia (IBEC), the Institute for Research in Biomedicine (IRB Barcelona) and the University of Barcelona (UB) announced that they had achieved photo-switchable, or light-regulated, molecules to control protein-protein interactions in a remote and non-invasive manner. The discovery signified a major step towards the development of targeted, light-controlled drugs, whose effects would be limited to a specific area and time, reducing side effects.

Now, in recent experiments published in the journal Chemistry & Biology, the group of researchers have been using their photo-sensitive molecules to control clathrin-mediated endocytosis, a process whereby cells absorb certain substances that they need to function properly. In doing so, theyʼve made a discovery that greatly expands the field of potential inhibitors, as it questions the need for the previously supposed rigid and helical structure of these molecules. In fact, researchers found that they donʼt require a rigid structure, and that flexible structures actually show a greater inhibitory capacity, as well as better photoswitching ability.

Further information

 

Article reference:

A. Martín-Quirós, L. Nevola, K. Eckelt, S. Madurga, P. Gorostiza and E. Giralt. "Absence of a stable secondary structure is not a limitation for photoswitchable inhibitors of b-arrestin/b-adaptin 2 protein-protein interaction". Chemistry & Biology, January 2015. DOI: 10.1016/j.chembiol.2014.10.022