Spotlight on the protein corona of liposomes
Liposomes are an established drug delivery platform that has paved the way to clinic for nanomedicine drugs. In the body, interactions of liposomes, as well as other drug delivery vehicles, are mediated by the complex dynamic layer of plasma proteins adsorbed on the surface, the protein corona. The review summarizes the data on liposome protein corona, tracing the path from interactions of individual proteins to the effects mediated by the corona in vivo. It critically assesses protein corona isolation and analysis techniques and offers a classification of the approaches to exploitation of the protein corona—rather than elimination thereof—based on the bilayer composition–protein corona composition–molecular interactions–biological performance relationship.
- Mechanism of coelenterazine chromophore photoinactivation from Beroe abissycola photoprotein is proposed
Scientists from IBCh RAS with colleagues from Photobiology Lab (IBP SB RAS) elucidated the structures of Beroe abissycola photoprotein’s chromophore photoinactivation products and proposed a mechanism of the photoinactivation process. The similarity of chemical transformations of photoprotein and GFP-like fluorescent protein chromophores was demonstrated for the first time. The results are published in Organic Letters. The project was funded by the RScF grant № 17-14-01169p.
- Essential role of zinc ions in TLR1 receptor activation
Toll-like receptors are the key players of the innate immune response. Despite the numerous studies and huge amount of data regarding these proteins, the structural basis of their functioning has not yet been clearly elucidated. Scientists from IBCh RAS, together with their colleagues from Moscow Institute of Physics and Technology and Changchun Institute of Applied Chemistry (China) discovered the essential role of zinc in the functioning of Toll-like receptor 1 and proposed possible mechanisms of zinc-mediated receptor activation. The work was funded by the RFBR grant 20-34-70024 and published in Communications Biology.
- New structural data allowed to study the mechanism of thermal activation of thermosensitive ion channels of the TRP family
Scientists from the Laboratory of biomolecular modeling of the IBCh RAS, together with colleagues from Columbia University (New York, USA), the University of Illinois (Peoria, USA), and the Institute of Physiology of the Czech Academy of Sciences (Prague, Czech Republic), have revealed the structural mechanism of heat-induced opening of temperature-sensitive TRP channels.