{"title":"Neuraminidase Inhibitory Activities of Some Alcoholic Plant Extracts and Chemical Compounds","authors":"Onur Ertik, Refiye Yanardag","doi":"10.3103/S0027131424700214","DOIUrl":"10.3103/S0027131424700214","url":null,"abstract":"<p>In today’s world, disease rates are increasing day after day because of environmental factors, lifestyles and technology. Although there are many drugs for many diseases, people’s interest and demand for herbal products are increasing. So, plants that can be used in the treatment of diseases have to be researched scientifically. Neuraminidase belongs to a class of glycosyl hydrolases that release terminal sialic acid from glycoproteins, glycolipids and polysaccharides. Neuraminidases could be found in animals, microorganisms and viruses. They have an impact on pathogenicity. This enzyme which is required for viral replication is a surface glycoprotein in influenza types A and B. In this study, we examined the inhibitory effects of some plant extracts and chemical compounds on neuraminidase activity. The result of our experiments indicates that the neuraminidase inhibitory activities of plant extracts and chemical compounds increased in a dose-dependent manner. We can conclude that the plant extracts and chemicals/drugs can be used in pharmaceutical industries and drug treatment due to their neuraminidase inhibitory activities.</p>","PeriodicalId":709,"journal":{"name":"Moscow University Chemistry Bulletin","volume":"79 3","pages":"225 - 231"},"PeriodicalIF":0.7,"publicationDate":"2024-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141609522","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
N. V. Rastriga, N. L. Eremeev, D. A. Klimov, P. A. Levashov
{"title":"Regulation of Enzyme-Dependent Lysis of Microbial Cells: Is the Effector Target an Enzyme or Substrate?","authors":"N. V. Rastriga, N. L. Eremeev, D. A. Klimov, P. A. Levashov","doi":"10.3103/S0027131424700172","DOIUrl":"10.3103/S0027131424700172","url":null,"abstract":"<p>In this study, an attempt is made to analyze the published data regarding the effectors of bacterial lysis in the presence of various bacteriolytic enzymes. Despite the differences between such enzymes, it is possible to identify certain general patterns of their action on a highly complex substrate—a living bacterial cell protected by a cell wall and additional complexes of biopolymers associated with it. Chicken and human lysozymes are the best known of these enzymes. They have some structural differences but are generally very similar in properties. Understanding the characteristics of the antibacterial action of bacteriolytic enzymes present both in medications and in the human immune system is extremely important for the development of new approaches to combat bacterial infections, including antibiotic-resistant ones. Moreover, certain logical and methodological approaches used to study bacteriolytic enzymes can be extremely useful for studying and describing other enzymes that affect complex polymer substrates in real biological situations.</p>","PeriodicalId":709,"journal":{"name":"Moscow University Chemistry Bulletin","volume":"79 3","pages":"195 - 202"},"PeriodicalIF":0.7,"publicationDate":"2024-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141614282","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
T. A. Bogush, A. A. Basharina, I. P. Romanov, A. N. Grishanina, E. A. Bogush, A. M. Scherbakov, A. B. Ravcheeva, A. Lee, V. S. Kosorukov
{"title":"Immunofluorescence Analysis of Estrogen Receptors Alpha Expression in Non-Small Cell Lung Cancer Tissue","authors":"T. A. Bogush, A. A. Basharina, I. P. Romanov, A. N. Grishanina, E. A. Bogush, A. M. Scherbakov, A. B. Ravcheeva, A. Lee, V. S. Kosorukov","doi":"10.3103/S0027131424700159","DOIUrl":"10.3103/S0027131424700159","url":null,"abstract":"<p>A quantitative assessment of the expression of estrogen receptors alpha (ERα) is carried out in 115 samples of non-small cell lung cancer (NSCLC) by an immunofluorescent assay and flow cytometry. It is shown that a high level of ERα of ≥20% predicts a higher aggressiveness of NSCLC than at a low level of <20%: median survival based on a follow-up period of 78 months increases by 1.5 times; the risk of death is reduced by a factor of almost 2.0 (<i>p</i> = 0.04). The time to death increases on average by 18 months in about 20% of patients with a low ERα expression. The results validate the informative value of the immunofluorescence analysis and flow cytometry for quantifying the ERα expression and substantiate the prospects of antiestrogen therapy as a new option for NSCLC treatment, in particular, by analogy with breast cancer—in a long-term adjuvant therapy in ERα<sup>+</sup> NSCLC patients.</p>","PeriodicalId":709,"journal":{"name":"Moscow University Chemistry Bulletin","volume":"79 3","pages":"182 - 188"},"PeriodicalIF":0.7,"publicationDate":"2024-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141614414","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Identification of “Hot Spots” to Improve Maturation of the moxSAASoti Fluorescent Protein at 37°C","authors":"N. K. Marynich, A. P. Savitsky","doi":"10.3103/S0027131424700196","DOIUrl":"10.3103/S0027131424700196","url":null,"abstract":"<p>A search for amino acid residues, whose replacement could contribute to the optimal maturation of the moxSAASoti fluorescent protein at 37°C, is carried out. For many other fluorescent proteins, this characteristic was improved by chance through many rounds of random mutagenesis; however, we managed to find two positions, 74 and 125, which clearly affect the process of moxSAASoti maturation, which is verified by introducing substitutions at these positions by site-directed and site-saturation mutagenesis.</p>","PeriodicalId":709,"journal":{"name":"Moscow University Chemistry Bulletin","volume":"79 3","pages":"211 - 216"},"PeriodicalIF":0.7,"publicationDate":"2024-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141614284","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
V. O. Ovsyannikov, A. Yu. Mikhailova, U. A. Budanova, Yu. L. Sebyakin
{"title":"Antibacterial Activity of Amphiphiles Based on Indolyl-3-Carboxylic Acids and L-Lysine with an Ethylenediamine Linker","authors":"V. O. Ovsyannikov, A. Yu. Mikhailova, U. A. Budanova, Yu. L. Sebyakin","doi":"10.3103/S0027131424700202","DOIUrl":"10.3103/S0027131424700202","url":null,"abstract":"<p>Recently, due to the growth in bacterial infections resistant to antibiotics, there is an urgent need for developing alternative antibacterial drugs. Alkyl-indolyl-L-lysines are a promising class of compounds; their amphiphilic structure is crucial in antimicrobial efficacy. A scheme is developed and five new derivatives of indolylbutyric and indolylacetic acids containing a polar amino acid residue with an ethylenediamine linker binding alkyl fragments with different lengths are synthesized. The antibacterial activity of the new amphiphiles against gram-positive and gram-negative bacterial strains is evaluated. The minimum binding energy of the synthesized compounds with human serum albumin (HSA) is determined by molecular docking. A lower affinity of the studied objects in comparison with control indolmycin is shown.</p>","PeriodicalId":709,"journal":{"name":"Moscow University Chemistry Bulletin","volume":"79 3","pages":"217 - 224"},"PeriodicalIF":0.7,"publicationDate":"2024-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141609521","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
I. V. Grigoryan, V. V. Spiridonov, A. M. Adelyanov, Yu. A. Koksharov, K. V. Potapenkov, I. V. Taranov, G. B. Khomutov, A. A. Yaroslavov
{"title":"New Magnetic Colloidal Systems Based on Biomimetic Polycomplexes","authors":"I. V. Grigoryan, V. V. Spiridonov, A. M. Adelyanov, Yu. A. Koksharov, K. V. Potapenkov, I. V. Taranov, G. B. Khomutov, A. A. Yaroslavov","doi":"10.3103/S0027131424700135","DOIUrl":"10.3103/S0027131424700135","url":null,"abstract":"<p>This paper presents new colloidal systems that have prospects for use as carriers of medicinal compounds and are polymer complexes based on polyacrylic acid molecules of various molecular weights and biogenic polyamine, additionally modified with magnetic iron oxide nanoparticles. The main physicochemical characteristics of the resulting polycomplexes are determined. The possibility of incorporating a doxorubicin medicinal compound in the polycomplexes is demonstrated, and the magnetic properties of the polycomplexes functionalized with magnetic iron oxide nanoparticles are studied.</p>","PeriodicalId":709,"journal":{"name":"Moscow University Chemistry Bulletin","volume":"79 3","pages":"170 - 174"},"PeriodicalIF":0.7,"publicationDate":"2024-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141614278","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
O. V. Maslova, O. V. Senko, N. A. Stepanov, I. V. Lyagin, E. N. Efremenko
{"title":"Biocatalysis in the Degradation of Synthetic Polymers","authors":"O. V. Maslova, O. V. Senko, N. A. Stepanov, I. V. Lyagin, E. N. Efremenko","doi":"10.3103/S0027131424700019","DOIUrl":"10.3103/S0027131424700019","url":null,"abstract":"<p>Waste from the production and use of synthetic polymers is a serious problem. The development of enzymatic and microbial biocatalysts capable of degrading hard-to-decompose polymers seems to be one of the promising and environmentally oriented solutions to this problem. A possibility of combining biocatalysts (BCs)—enzymes and microbial cells—with metal catalysts is considered as a promising basis for the development of new hybrid chemobiocatalytic processes intended for the effective degradation of synthetic polymers (SPs).</p>","PeriodicalId":709,"journal":{"name":"Moscow University Chemistry Bulletin","volume":"79 2","pages":"140 - 145"},"PeriodicalIF":0.7,"publicationDate":"2024-06-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141513810","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Strategies of N-Glycosidic Bond Cleavage by DNA Repair Enzymes","authors":"A. V. Endutkin, D. O. Zharkov","doi":"10.3103/S0027131424700044","DOIUrl":"10.3103/S0027131424700044","url":null,"abstract":"<p>DNA glycosylases are enzymes that hydrolyze the <i>N-</i>glycosidic bond of damaged nucleotides, initiating the process of base excision DNA repair. There are at least eight structural classes of these enzymes, differing in both their substrate specificity and the mechanism of catalysis. The review examines the mechanisms of human and bacterial DNA glycosylases that protect the genome from the major types of DNA damage.</p>","PeriodicalId":709,"journal":{"name":"Moscow University Chemistry Bulletin","volume":"79 2","pages":"121 - 126"},"PeriodicalIF":0.7,"publicationDate":"2024-06-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141548875","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Protein Engineering of Lactate Oxidase","authors":"E. D. Belyaeva, N. V. Komarova, A. E. Kuznetsov","doi":"10.3103/S0027131424700032","DOIUrl":"10.3103/S0027131424700032","url":null,"abstract":"<p>Lactate oxidase is a practically important enzyme widely used to detect L-lactate in medical diagnostics and in the food industry. This review summarizes the results of protein engineering of lactate oxidases to clarify the underlying mechanism of action of the enzyme and to improve its performance properties.</p>","PeriodicalId":709,"journal":{"name":"Moscow University Chemistry Bulletin","volume":"79 2","pages":"127 - 132"},"PeriodicalIF":0.7,"publicationDate":"2024-06-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141548878","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
A. M. Rozhkova, Yu. A. Denisenko, I. G. Sinelnikov, I. N. Zorov, D. V. Erokhin, V. G. Dzhavakhia
{"title":"Application of MF3 Microbial Recombinant Protein in Refolding of Plant Chitinase","authors":"A. M. Rozhkova, Yu. A. Denisenko, I. G. Sinelnikov, I. N. Zorov, D. V. Erokhin, V. G. Dzhavakhia","doi":"10.3103/S0027131424700020","DOIUrl":"10.3103/S0027131424700020","url":null,"abstract":"<p>Expression of recombinant proteins is important for studying their biological functions. For the primary description of protein properties, the <i>E. coli</i> expression system is most often used. However, in overexpression conditions, the rate of aggregation of target proteins often exceeds the rate of proper folding, resulting in the formation of insoluble inclusion bodies. Inclusion bodies are a clear disadvantage of the <i>E. coli</i> expression system since they prevent the extraction of target recombinant proteins. The use of chaperone-like proteins in vitro while refolding a target protein is one of the solutions to the existing problem. In this study, the MF3 recombinant protein is an example of a chaperone-like protein, which increases the yield of soluble plant chitinase by 92% compared to the yield of this protein using the standard refolding procedure.</p>","PeriodicalId":709,"journal":{"name":"Moscow University Chemistry Bulletin","volume":"79 2","pages":"133 - 139"},"PeriodicalIF":0.7,"publicationDate":"2024-06-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141513809","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}