The current research activity in the Molecular Biophysics Laboratory group focuses on the following main topics:

- Interaction of drugs with lipid bilayers and transport proteins

This research topic regards the interaction of exogenous (pharmacological) molecules with the cell membrane components, i.e., lipids and proteins. We focus on ligands of biomedical interest such as ibuprofen, a nonsteroidal anti-inflammatory drug widely used as a therapeutic agents worldwide for pain treatment and for its antipyretic and analgesic activities. It is well recognized that both the physiological activity and side effects of drug on human health may involve an interaction with cell membranes. For our study, we characterize their influence on membrane model systems made up of phosphatidylcholine molecules, which is the most abundant phospholipid in eukaryotic cells, and human serum albumin (HSA), the most abundant transport protein in the blood plasma. The research activity are carried out by combining an array of appropriate experimental and computational approaches.

- Structure and dynamics of biosystems at cryogenic temperature

This research line is in the frame of cryo-biophysics and it concerns with the structural, dynamical and molecular investigation of biosystems that are cryogenically frozen at low temperature. Our aim is to study the glassy-behavior shown by lipids and proteins at around 200 K and to characterize the librational motion that drive the low temperature phase behavior. To this end, we jointly use conventional and echo detected EPR spectra of chain labelled lipids in lamellar phases formed by glycerophospholipids in the temperature range between 77 and 260 K. In particular, we focus on ester- and ether-linked phosphatidylcholines that form bilayers with noninterdigitated chains and lamellar phases with interdigitated chains, respectively.

- Functional properties of intrinsically disordered proteins

This research topic regards the functional properties of intrinsically disordered proteins. These proteins form a specific class of polypeptides that do not have stable secondary or tertiary structures in several regions, or throughout their whole sequence, since they exist as an ensemble of rapidly inter-converting structures. Because of their plasticity, disordered proteins act as hubs in interaction networks carrying out several functions in cell-signaling routes and regulation, and they are very often involved in important diseases. Intrinsically disordered proteins are present in all kingdoms of life: in eukaryotic cells, more than 40% of the proteins possess disordered regions longer than 50 amino acid residues. Thus, understanding their function is highly interesting and quite challenging.