Using synchrotron light, a study led by CIC bioGUNE has described a molecular recognition mechanism which enables certain proteins of our cells to be recycled and reused. The results, published in Cell journal, open the door to biomedical applications for the treatment of pathologies like Alzheimer or Parkinson.
Artax Biopharma (Cambridge, MA), has successfully solved the crystal structure of its target protein by using X-ray diffraction at the XALOC beamline of the ALBA Synchrotron.
The research was led by Salvador Ventura, from the IBB-Department of Biochemistry at the UAB, and SOM Biotech, a biopharmaceutical company that discovered the use of tolcapone for treating ATTR and holds the patent on it. The crystal structure of TTRtolcalpone was solved by the group of David Reverter, at the IBB-UAB, in collaboration with the XALOC beamline scientists.
A team of scientists from CIC bioGUNE, University of Liverpool and Cedars-Sinai hospital in California, using high-resolution structures, have determined the catalytic steps of the enzyme MATα2. This study, with data collected at the ALBA Synchrotron, opens up a new pathway in the development of highly targeted drugs that act exclusively on this enzyme, regulating cancer cell growth.
Using ALBA and ESRF X-rays, researchers were able to solve the structure of the fibre head of turkey adenovirus 3 (TAdV-3), which causes fatal hemorrhagic enteritis in turkeys.
