Institute of
bioorganic chemistry

Scientists from the Department of Chemical Biology of Glycans and Lipids, the Department of structural biology and the Department of Biomaterials and Bionanotechnology IBCh RAS in collaboration with Russian and foreign colleges published a paper in ChemistryOpen on the study of conjugate of a biotin with DOPE (dioleoylphosphatidyl ethanolamine) through a nontrivial spacer, CMG (made from oligoglycine, some of glycines are carboxymethylated). biot-CMG-DOPE remarkably integrates into living cells, and in seconds (by simple contact) it covers almost any surface - and this has become a universal way of biotinylation. The work sheds light on the supramolecular organization of biot-CMG-DOPE molecule as part of the cell membrane and the mechanism of its interaction with streptavidin. Learn more

Scientists from the Laboratory of bioengineering of neuromodulators and neuroreceptors, the Laboratory of structural biology of ion channels and the Laboratory of neuroreceptors and neuroregulators Shemyakin-Ovchnnikov Institute together with colleagues from the Faculty of biology of Moscow State University and other russian scientific institutes, found that the intranasal administration of the water-soluble analogue of the human neuromodulator Lynx1, which is a GPI-tethered regulatory protein colocalized with nicotinic acetylcholine receptors (nAChRs) in the brain regions responsible for learning and memory can prevent cognitive impairment associated with dysfunction of the α7 type nicotinic acetylcholine receptor. The work is published in the Journal of Neurochemistry under support of Russian Science Foundation. Learn more

Researchers from the Group of in silico analysis of membrane proteins structure and the Laboratory of biomolecular modeling of IBCh RAS have predicted the structure of the complex between lantibiotic nisin with the bacterial cell wall precursor — lipid II — on the membrane surface. Using molecular simulations it was demonstrated that the high selectivity of nisin/lipid II interaction is explained by the ability of lipid II’s pyrophosphate group to form a pharmacophore on the bilayer surface that cannot be formed by phospholipids. It was shown that molecular recognition occurs via the induced-fit mechanism and is determined by the properties of the environment. Only one or two states within the conformational ensembles of both partners were found to be suitable for complex formation. These results may be employed for further development of new nisin-based antibiotics. The study is published in Scientific Reports. Learn more

The new research about metal nanoclusters performed by a team of authors from the Scientific Clinical Center for Physico-Chemical Medicine, Moscow Institute of Physics and Technology and IBCh RAS was recently published in Materials and Design journal. Metal nanoclusters, consisting of several tens of metal atoms and having a size of less than 2 nm, are a promising material due to their unique optical properties that appear due to the splitting of electron energy spectrum in metal into discrete energy levels as a result of quantum-size effects. The researchers of the Electron microscopy group of our institute carried out an important part of the work on direct visualization of the obtained structures, as well as on the measurement of energy dispersive X-ray spectra. Learn more

Researchers of the Laboratory of plant functional genomics and proteomics, IBCh RAS, in collaboration with Laboratory of molecular basis of plant stress resistance, IBCh RAS, and James Hutton Institute (United Kingdom) published a review article in the international peer-reviewed scientific journal New Phytologist (IF = 7.29). This review “The role of chloroplast protein remodeling in stress responses and shaping of the plant peptidome” is focused on processes of reorganization of the chloroplast proteome under stress conditions and on the roles of bioactive peptides generated from chloroplast proteins. This work was supported by the Government of Russian Federation Grant No. 14.W03.31.0003. Learn more