Through the microscope: TMEM16F protein and its molecular dance

The study was recently published in Nature Communications
membrane protein

TMEM16F, a membrane protein involved in several crucial biological processes, including blood coagulation and Covid-19 pathogenesis, has been the focus of an innovative study conceived and led by a team of researchers and former PhD students from SISSA in collaboration with other institutions such as the University of Zurich and the Nano Life Science Institute at the University of Kanazawa. Membrane proteins, including TMEM16F, constitute a particularly complex field of study. To fully comprehend their structure and function, it is necessary to study them in their native environment. Using cutting-edge techniques such as singlemolecule force spectroscopy (SMFS) and high-speed atomic force microscopy (HS-AFM), the team has unveiled new insights into the complex structural dynamics of TMEM16F. The results of this study, published in Nature Communications, open new pathways in medical research and could lead to the development of targeted therapies for diseases linked to the functioning of membrane proteins. 

Membrane proteins, as suggested by their name, are proteins found in cell membranes and play a key role in regulating cell functions, from nutrient transport to immune defence. However, studying these biological structures in their native environment is a complex challenge. In 2022, a group of researchers at SISSA overcame this difficulty by introducing an innovative approach that leverages artificial intelligence and atomic force microscopy. This new method allows for the study of the properties and mechanical stability of membrane proteins in their physiological conditions without the need for isolation.