Laboratory of Peptide Chemistry
Head of the Lab
Margarita Monastyrnaya, D.Sc.
Lab staff
Emma Kozlovskaya (Major Researcher, D.Sc.), Elena Zelepuga (Senior Researcher, Ph.D.)
Main research areas
Venomous marine cnidarians, sea anemones are a unique source of polypeptides, such as neurotoxins, pore-forming toxins (actinoporins), toxic APETx2-like peptides and polyfunctional polypeptides of Kunitz-type, whose functional activity associated with performing in the organism-producer allomonal role. With the help of these polypeptides, the sea anemones are protected from potential enemies and/or use them to attack the prey. Venom polypeptide components can selectively activate or block certain physiologically important for the body ion channels and ionotropic receptors, thereby modulating their functional activity and exhibiting a therapeutic effect. So, molecular targets of action of neurotoxins are voltage gating Na+-channels of different types, ones of actinoporins – the cytoplasmic sphingomyelin-containing membrane of eukaryotic cells, ones of toxic APETx2-like peptides – the acid-susceptible Na+-channels, ASICs, ones of polyfunctional Kunitz-type polypeptides – serine proteases and, in some cases, polyfunctional vanilloid TRPV1 receptor. It is shown that both actinoporins and Kunitz-type polypeptides are members of multigene families forming so-called combinatorial libraries of highly homologous molecules.
Laboratory of peptide chemistry staff conduct a comprehensive study of the sea anemones polypeptide components, develop approaches for their identification, isolation, structural and functional analysis. A bioinformatic search of polypeptides and peptides exhibiting high specificity for pain ionotropic receptors and ion channels involved in the processes of perception, processing and transmission of signals in the central nervous system is actively conducted.
bioinformatic
The main goals
The study of structure-functional interaction of the sea anemone toxic polypeptides (2 type neurotoxins, actinoporins, polypeptides of Kunitz-type and APETx2-like toxic peptides) by methods of structure protein chemistry, molecular biology, bioinformatics, electrophysiology and biophysics. ïîëó÷åíèå
Highlights and perspectives
In silico investigation of protein-protein relationships of actinoporins, APETx2-like toxic peptides and polypeptides of Kunitz-type with their biological targets.
Obtaining of functionally active recombinants of Kunitz-type polypeptides with the aim of in vivo and in vitro investigation of their pharmaceutical potential.
Laboratory of peptide chemistry staff conduct a comprehensive study of the sea anemones polypeptide components, develop approaches for their identification, isolation, structural and functional analysis. A bioinformatic search of polypeptides and peptides exhibiting high specificity for pain ionotropic receptors and ion channels involved in the processes of perception, processing and transmission of signals in the central nervous system is actively conducted.
bioinformatic
The main goals
The study of structure-functional interaction of the sea anemone toxic polypeptides (2 type neurotoxins, actinoporins, polypeptides of Kunitz-type and APETx2-like toxic peptides) by methods of structure protein chemistry, molecular biology, bioinformatics, electrophysiology and biophysics. ïîëó÷åíèå
Highlights and perspectives
In silico investigation of protein-protein relationships of actinoporins, APETx2-like toxic peptides and polypeptides of Kunitz-type with their biological targets.
Obtaining of functionally active recombinants of Kunitz-type polypeptides with the aim of in vivo and in vitro investigation of their pharmaceutical potential.