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}
{"title":"Protein Engineering of Bst Polymerase for Isothermal Amplification Purposes","authors":"A. S. Cherkashina, O. O. Mikheeva, V. G. Akimkin","doi":"10.3103/S002713142470007X","DOIUrl":"10.3103/S002713142470007X","url":null,"abstract":"<p>This paper reviews the protein engineering of Bst polymerase using various methods. To modify the enzyme, approaches such as the production of chimeric proteins, directed evolution, and directed and random mutagenesis are used. Examples of successful changes in enzyme properties such as catalytic activity, processivity, thermal stability, and resistance to inhibitors are described.</p>","PeriodicalId":709,"journal":{"name":"Moscow University Chemistry Bulletin","volume":"79 2","pages":"105 - 109"},"PeriodicalIF":0.7,"publicationDate":"2024-06-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141548873","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}
D. M. Hushpulian, I. N. Gaisina, S. V. Nikulin, T. A. Chubar, S. S. Savin, I. G. Gazaryan, V. I. Tishkov
{"title":"High Throughput Screening in Drug Discovery: Problems and Solutions","authors":"D. M. Hushpulian, I. N. Gaisina, S. V. Nikulin, T. A. Chubar, S. S. Savin, I. G. Gazaryan, V. I. Tishkov","doi":"10.3103/S0027131424700081","DOIUrl":"10.3103/S0027131424700081","url":null,"abstract":"<p>World-wide introduction of high throughput screening (HTS) methods in drug discovery research did not result in the increased number of novel medications on the market. We discuss novel trends in drug discovery that came from the understanding that majority of diseases are multifactorial and that one enzyme has many protein substrates. Hence, new approaches are focused on development of drugs, which (1) trigger survival pathways to return the organism to homeostatic balance, and (2) inhibit enzymes modifying histones or transcription factors not at the active site, but by displacement of protein substrates from the enzyme complexes. A good example for both approaches comes from the development of activators of antioxidant defense. We analyze and illustrate problems of commonly used in vitro HTS assays, and briefly discuss advantages and limitations of small animal models. The novel approaches are complementary to the standard HTS and do not substitute for testing in mammals. Development of transgenic reporter mice to monitor drug effects by means of in vivo imaging is extremely promising to select proper dosage and administration regimes for full-range PK studies.</p>","PeriodicalId":709,"journal":{"name":"Moscow University Chemistry Bulletin","volume":"79 2","pages":"93 - 104"},"PeriodicalIF":0.7,"publicationDate":"2024-06-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141548877","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}