Oxana Galzitskaya*
Gamaleya Research Centre of Epidemiology and Microbiology
ogalzit [at] vega.protres.ru
Abstract
Studying the fundamental principles of protein self-organization has enabled us to address important applied problems, such as developing new antimicrobial peptides, determining the composition of amyloid deposits for patients, and participating in a project to develop cancer and HIV vaccines.
Based on the co-aggregation model, new antibacterial peptides have been created against the pathogens Pseudomonas aeruginosa and Staphylococcus aureus. The innovative peptide should interact with the target protein of the model or pathogenic bacteria, forming aggregates and removing this protein, which is essential for the life of the bacteria, from its active state. Synergistic effects have been demonstrated for several peptides.
We discovered a new mutation in lysozyme amyloidosis with the amino acid substitution p.F21L/T88N, found in a Russian family, and correct typing of the amyloidosis saved the lives of two patients.
We studied the influence of physicochemical properties (hydrophobicity, net charge, aliphatic index, instability index, isoelectric point, molecular weight, etc.) on the non-covalent interaction of human epitopes with polymorphic proteins of the major histocompatibility complex class I (MHC I). The structural characteristics of this interaction are important in studying the immunogenicity of epitopes, as well as in the development of multi-epitope peptide vaccines. We developed an AI-based method for determining the binding of potential neoepitopes to a given MHC I complex and assessing its immunogenicity.
Keywords: amyloids, antimicrobial peptide, neoantigen, vaccine