Screening of the promising direct thrombin inhibitors from haematophagous organisms. Part I: Recombinant analogues and their antithrombotic activity in vitro
This is a collaborative work of researchers from the Laboratory of Biopharmaceutical Technologies of the IBCh RAS and Biological Testing Laboratory of the BIBCh RAS. Its goal is the development and testing of new anticoagulants from haematophagous organisms. Haemadin from the leech Haemadipsa sylvestris, variegin from the tick Amblyomma variegatum, and anophelin from Anopheles albimanus were chosen as the most promising anticoagulants. We have developed a method for the biotechnological production of these recombinant peptides with pharmaceutical purity. As a reference standard, we have used the recombinant hirudin-1 from Hirudo medicinalis (desirudin), which is the active substance of the FDA-approved drug Iprivask (Aventis Pharmaceuticals, USA). The anticoagulant activities of these peptides were compared using the thrombin amidolytic activity assay and detection of the prolongation of coagulation time (thrombin time, prothrombin time, and activated partial thromboplastin time) in mouse and human plasma. The article was published in the journal Biomedicines (IF 6.081).
- Capsule-Targeting Depolymerases Derived from Acinetobacter baumannii Prophage Regions
A team of scientists from the Laboratory of molecular bioengineering IBCh RAS together with the colleagues from other Russian Institutes bioinformatically predicted and recombinantly produced several different depolymerases encoded in the prophage regions of Acinetobacter baumannii genomes. For two depolymerases, the specificity to capsular polysaccharides (CPSs) of A. baumannii belonging to K1 and K92 capsular types (K types) was determined. These enzymes can be considered as suitable candidates for the development of new antibacterials against corresponding A. baumannii K types.
- Evolution of Phage Tail Sheath Protein
A team of scientists from the Laboratory of molecular bioengineering IBCh RAS analysed 112 contractile phage tail sheath proteins (TShP) representing different groups of bacteriophages and archaeal viruses with myoviral morphology have been modelled with the novel machine learning software, AlphaFold 2. The common core domain of all studied sheath proteins, including viral and T6SS proteins, comprised both N-terminal and C-terminal parts, whereas the other parts consisted of one or several moderately conserved domains, presumably added during phage evolution.
- Heterogeneity of the GFP fitness landscape and data-driven protein design
Understanding the relationship between genotype and phenotype, the fitness landscape, elucidates the fundamental laws of heredity (Canale et al. 2018) and may ultimately create novel methods of protein design (Alley et al. 2019). The fitness landscape is often conceptualised as a multidimensional surface (Kondrashov and Kondrashov, 2015) with one dimension representing fitness, or another phenotype, and the other dimensions each representing a genotype’s locus.
- Seminar “Molecular brain”: Allan Kalueff
V.12 (This event is over)
Seminar “Molecular brain” resumes its work after the long delay caused by pandemic of new coronavirus infection. However, all the people who are liking to listen lectures on-line, can participate via zoom-translation (link). The seminar will be held on the 12th of May at 3 pm in the Small lecture hall (3rd floor, BON, IBCh). Everyone is welcome!
- Gene therapy 2.0: AAV beyond monogenic gene correction
II.4–5 (This event is over)
Founding and managing partner of 4BIO Capital - Dmitry Kuzmin - will make a presentation in conference room 04 Februry 2022 at 15:00