The Protein Journal最新文献

{"title":"Inhibitor Action of Unsaturated Fatty Acids on Equine Serum Butyrylcholinesterase","authors":"Mehmet Berk Akay,&nbsp;Kubra Sener,&nbsp;Suat Sari,&nbsp;Ebru Bodur","doi":"10.1007/s10930-025-10259-8","DOIUrl":"10.1007/s10930-025-10259-8","url":null,"abstract":"<div><p>Butyrylcholinesterase (BChE; EC 3.1.1.8), a serine hydrolase found in various tissues, hydrolyses choline esters such as acetylcholine and succinylcholine, as well as other esters such as heroin and acetylsalicylic acid. It is considered to play a role in lipid metabolism as it belongs to the same enzyme group as lipases and its catalytic subunits are similar. In this study, the effects of unsaturated fatty acids, namely arachidonic (AA), linoleic (LA), alpha-linolenic (ALA) and oleic acid (OA), on equine serum BChE (EqBChE) were investigated. Enzyme activity was measured by the modified Ellman method. When the activity results were evaluated, the IC50 values were found 45.49, 8.465, 1556, and 56.57 μM; while the Ki values were 63.92, 11.46, 1800, and 15.24 μM for AA, ALA, LA, and OA, respectively. Analysis of the kinetic results showed that ALA was compatible with mixed inhibition and other fatty acids were compatible with non-competitive inhibition, a special type of mixed inhibition. Molecular docking predicted binding of the fatty acids to the active site, as well as to predicted allosteric sites. The results of this study provide another support to the hypothesis that cholinesterases are associated with lipid metabolism.</p></div>","PeriodicalId":793,"journal":{"name":"The Protein Journal","volume":"44 3","pages":"271 - 282"},"PeriodicalIF":1.4,"publicationDate":"2025-02-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143476520","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Effects of Heavy Metal Stress on Seedling Growth and Antioxidant System in Sorghum (Sorghum Bicolor (L.) Moench)","authors":"Büşra Çevık,&nbsp;Hakan Arslan,&nbsp;Deniz Ekinci","doi":"10.1007/s10930-025-10258-9","DOIUrl":"10.1007/s10930-025-10258-9","url":null,"abstract":"<div><p>Factors that impede the normal growth and development of plants are termed ‘stress factors’ and result in yield loss. Exposure to elevated concentrations of heavy metals has been demonstrated to induce the production of reactive oxygen species (ROS), which can affect physiological and biochemical processes. The present study investigated the effects of two common heavy metals (Hg²⁺ and Cd²⁺) on specific physiological and biochemical parameters of sorghum (<i>Sorghum bicolor</i> (L.) Moench). The study utilized doses ranging from 3 to 15 ppm for the application of heavy metals. The study focused on the effects of these metals on the activities of enzymes (superoxide dismutase and peroxidase), chlorophyll content, fresh weight, dry weight, and proline content in sorghum plants. The study found that applying mercury at 9 ppm resulted in the highest activity of peroxidase (POX), with an observed increase of 69.57% compared to the control. Conversely, cadmium application at 12 ppm elicited the highest activity, increasing by 102.17% compared to the control. For superoxide dismutase (SOD), the peak activity was observed at 6 ppm for both applications, with an increase of 84.16% in the mercury application control group and 121.08% in the cadmium application group compared to the control group. A similar pattern was observed in the chlorophyll content, which initially increased and then decreased. Declines in fresh weight, dry weight, and proline accumulation were also documented.</p></div>","PeriodicalId":793,"journal":{"name":"The Protein Journal","volume":"44 3","pages":"308 - 316"},"PeriodicalIF":1.4,"publicationDate":"2025-02-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143476552","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Functional and Biochemical Analyses of Glycerol Kinase and Glycerol 3-phosphate Dehydrogenase in HEK293 Cells","authors":"Superior Syngkli,&nbsp;Sumit K. Singh,&nbsp;Riva M. Rani,&nbsp;Bidyadhar Das","doi":"10.1007/s10930-025-10252-1","DOIUrl":"10.1007/s10930-025-10252-1","url":null,"abstract":"<div><p>Type 2 diabetes mellitus (T2DM) is a chronic metabolic disorder and its concurrent presence with chronic kidney disease (CKD) is a significant concern. Glycerol kinase (GK) and glycerol 3-phosphate shuttle enzymes (cGPDH and mGPDH) facilitate the regulation of endogenous glucose production in many cell lines. This research investigates the functions of GK, cGPDH, and mGPDH in HEK293 cells. Standard protocols were employed to assess enzyme activity, mRNA- and protein-expression, glucose uptake, and production. Homology modeling and molecular docking were employed to elucidate interactions of genistein and metformin with these enzymes. The secondary structures of GK, cGPDH and mGPDH and the thermal stability of cGPDH and mGPDH were analyzed by CD spectra. Genistein inhibited GK activity by 40%, while metformin decreased cGPDH and mGPDH activity by 58% and 55%, respectively, in HEK293 cells. Nonetheless, the expression levels of mRNA and protein remained unaltered. Genistein and metformin inhibited HEK293 glucose production by 0.46-fold and 0.63-fold, respectively. Genistein reduced glucose uptake by 0.26-fold, while metformin increased it by 0.51-fold. Genistein allosterically interacted with GK with a CDocker energy of -27.71, while metformin interacted with Gln295 and Lys296 of the catalytic loop of cGPDH and the FAD⁺ binding domain of mGPDH, yielding CDocker energies of -11.12 and -13.34, respectively. This study indicated the role of genistein and metformin on GK, cGPDH, and mGPDH in HEK293 cells.</p></div>","PeriodicalId":793,"journal":{"name":"The Protein Journal","volume":"44 2","pages":"231 - 244"},"PeriodicalIF":1.9,"publicationDate":"2025-02-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143476518","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Pfs16: A Key Parasitophorous Vacuole Membrane Protein Crucial for Malaria Parasite Development and Transmission","authors":"Sadeq Shabani,&nbsp;Laura Renee Serbus","doi":"10.1007/s10930-025-10260-1","DOIUrl":"10.1007/s10930-025-10260-1","url":null,"abstract":"<div><p>Malaria remains a formidable challenge to global health, claiming the lives of nearly half a million individuals annually despite vigorous efforts to curb its spread. Among the myriad factors influencing the persistence and virulence of this disease, the role of specific proteins during the Plasmodium development cycle is critical. The protein of interest, Pfs16, is a Parasitophorous Vacuole Membrane Protein expressed from the earliest asexual stages, which encompass the development of <i>Plasmodium falciparum</i> in the host, to the final stage of the parasite's development in the mosquito, the sporozoite, playing a crucial role in this lifecycle. Understanding the function and mechanism of this conserved protein is pivotal for advancing our strategies to combat malaria. In this review, we examine the work on Pfs16 in both the asexual and sexual stages of parasite development, aiming to gain a better understanding of this protein as a promising candidate for drug and vaccine development.</p></div>","PeriodicalId":793,"journal":{"name":"The Protein Journal","volume":"44 2","pages":"133 - 146"},"PeriodicalIF":1.9,"publicationDate":"2025-02-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143470419","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Biochemical Characterization of a Novel Cysteine Protease Purified from the Medicinal Plant Kaempferia galanga L.","authors":"Jasmi Ningthoujam,&nbsp;Mayashree Borthakur Syiem,&nbsp;Donkupar Syiem","doi":"10.1007/s10930-025-10255-y","DOIUrl":"10.1007/s10930-025-10255-y","url":null,"abstract":"<div><p>Plant-derived cysteine proteases have emerged as a compelling subject of investigation, capturing scientific interest owing to their potential applications in diverse industries, including food and biotechnology. This study focused on isolating <i>Kaempferia galanga</i> cysteine protease (KgCP) from rhizomes of <i>Kaempferia galanga</i>, followed by a comprehensive characterization of the protease. It was purified and characterized using various biochemical and biophysical techniques, including anion-exchange chromatography, gel filtration, SDS-PAGE electrophoresis, and enzyme assays. With a yield of 23.2%, the purification process generated a 6.03-fold increase in specific activity. KgCP’s molecular weight was determined to be around 33 kDa and exhibited optimal catalytic performance at 55 °C and pH 5.5. Values of its catalytic parameters, <i>V</i>_max and <i>K</i>_m, were found to be 103.7 Units min⁻¹ and 0.025 μmol, respectively. Inhibition of KgCP by various cysteine protease inhibitors – E-64, iodoacetamide, and mercury chloride confirmed it to be a cysteine protease. The inclusion of detergents and organic solvents did not affect the stability of KgCP. Although proteolytic activity was compromised by metal ions such as Cd²⁺, Co²⁺, and Fe³⁺, other metal ions (Ca²⁺, Mg²⁺, Mn²⁺, Sn²⁺, Sr²⁺, etc.) showed negligible impact on its proteolytic activity. These findings expand our understanding of the biological characteristics of this cysteine protease, highlighting its potential for applications in the dairy industry, bioactive peptide synthesis, detergents industry, etc. The entire work can be graphically presented as follows:</p><h3>Graphical abstract</h3>\u0000<div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":793,"journal":{"name":"The Protein Journal","volume":"44 2","pages":"213 - 230"},"PeriodicalIF":1.9,"publicationDate":"2025-02-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143470417","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"An Analysis of Intrinsic Protein Disorder in Antimicrobial Peptides","authors":"Michael Antonietti,&nbsp;Colin K. Kim,&nbsp;Sydney Granack,&nbsp;Nedym Hadzijahic,&nbsp;David J. Taylor Gonzalez,&nbsp;William R. Herskowitz,&nbsp;Vladimir N. Uversky,&nbsp;Mak B. Djulbegovic","doi":"10.1007/s10930-025-10253-0","DOIUrl":"10.1007/s10930-025-10253-0","url":null,"abstract":"<div><p>Antibiotic resistance, driven by the rise of pathogens like VRE and MRSA, poses a global health threat, prompting the exploration of antimicrobial peptides (AMPs) as alternatives to traditional antibiotics. AMPs, known for their broad-spectrum activity and structural flexibility, share characteristics with intrinsically disordered proteins, which lack a rigid structure and play diverse roles in cellular processes. This study aims to quantify the intrinsic disorder and liquid–liquid phase separation (LLPS) propensity in AMPs, advancing our understanding of their antimicrobial mechanisms and potential therapeutic applications. To investigate the propensity for intrinsic disorder and LLPS in AMPs, we compared the AMPs to the human proteome. The AMP sequences were retrieved from the AMP database (APD3), while the human proteome was obtained from the UniProt database. We analyzed amino acid composition using the Composition Profiler tool and assessed intrinsic disorder using various predictors, including PONDR® and IUPred, through the Rapid Intrinsic Disorder Analysis Online (RIDAO) platform. For LLPS propensity, we employed FuzDrop, and FuzPred was used to predict context-dependent binding behaviors. Statistical analyses, such as ANOVA and χ² tests, were performed to determine the significance of observed differences between the two groups. We analyzed over 3000 AMPs and 20,000 human proteins to investigate differences in amino acid composition, intrinsic disorder, and LLPS potential. Composition analysis revealed distinct differences in amino acid abundance, with AMPs showing an enrichment in both order-promoting and disorder-promoting amino acids compared to the human proteome. Intrinsic disorder analysis, performed using a range of predictors, consistently demonstrated that AMPs exhibit higher levels of predicted disorder than human proteins, with significant differences confirmed by statistical tests. LLPS analysis, conducted using FuzDrop, showed that AMPs had a lower overall propensity for LLPS compared to human proteins, although specific subsets of AMPs exhibited high LLPS potential. Additionally, redox-dependent disorder predictions highlighted significant differences in how AMP and human proteins respond to oxidative conditions, further suggesting functional divergences between the two proteomes. CH-CDF plot analysis revealed that AMPs and human proteins occupy distinct structural categories, with AMPs showing a greater proportion of highly disordered proteins compared to the human proteome. These findings underscore key molecular differences between AMPs and human proteins, with implications for their antimicrobial activity and potential therapeutic applications. Our study reveals that AMPs possess a significantly higher degree of intrinsic disorder and specific subsets exhibit LLPS potential, distinguishing them from the human proteome. These molecular characteristics likely contribute to their antimicrobial function an","PeriodicalId":793,"journal":{"name":"The Protein Journal","volume":"44 2","pages":"175 - 191"},"PeriodicalIF":1.9,"publicationDate":"2025-02-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s10930-025-10253-0.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143470415","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Crystal Structure of a Thioredoxin-like Ferredoxin Encoded Within a Cobalamin Biosynthetic Operon of Rhodobacter capsulatus","authors":"Yan-Hao Shen,&nbsp;Wen-Long Cheng,&nbsp;Xiao Wang,&nbsp;Huai-En Dai,&nbsp;Mingzhu Wang,&nbsp;Lin Liu","doi":"10.1007/s10930-025-10254-z","DOIUrl":"10.1007/s10930-025-10254-z","url":null,"abstract":"<div><p>Thioredoxin-like ferredoxin is a small homodimeric protein containing a [2Fe-2S] cluster in each monomer. It is only found in bacteria but its physiological function remains largely unknown. The cobalamin biosynthetic operon in the genome of the purple phototroph <i>Rhodobacter capsulatus</i> encodes a putative ferredoxin dubbed as CfrX. To characterize this protein, we cloned, expressed, purified, and crystalized the recombinant CfrX in the iron-sulfur cluster-bound state, and solved the structure at 2.1-Å resolution. Adopting a typical thioredoxin-like ferredoxin fold, a CfrX monomer binds one [2Fe-2S] cluster through four Cys residues located on two protruding loops. Unexpectedly, CfrX dimerizes in a previously unreported manner. With the structural information, we ascertained CfrX as a thioredoxin-like ferredoxin. While the precise function of CfrX in cobalamin biosynthesis is elusive, a link between CfrX and aerobic cobaltochelatase should exist due to the gene clustering pattern. We also discussed the possible relationship among CfrX, CobW, and CobNST with respect to the [2Fe-2S] cluster.</p></div>","PeriodicalId":793,"journal":{"name":"The Protein Journal","volume":"44 2","pages":"192 - 200"},"PeriodicalIF":1.9,"publicationDate":"2025-02-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143384621","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Lipid Transfer Proteins (LTPs) Partially Purified from Capsicum chinense Jacq. Seeds: Antifungal Properties and α-amylase Inhibitory Activity","authors":"Arielle Pinheiro Bessiatti Fava Oliveira,&nbsp;Larissa Maximiano Resende,&nbsp;Marciele Souza da Silva,&nbsp;Layrana de Azevedo dos Santos,&nbsp;André Oliveira Carvalho,&nbsp;Renata Pinheiro Chaves,&nbsp;Celso Shiniti Nagano,&nbsp;Felipe Figueirôa Moreira,&nbsp;Sérgio Henrique Seabra,&nbsp;Maura Da Cunha,&nbsp;Érica de Oliveira Mello,&nbsp;Gabriel Bonan Taveira,&nbsp;Rosana Rodrigues,&nbsp;Valdirene Moreira Gomes","doi":"10.1007/s10930-025-10256-x","DOIUrl":"10.1007/s10930-025-10256-x","url":null,"abstract":"<div><p>In this study, we identified and partially purified antimicrobial peptides belonging to the family of lipid transfer proteins (LTPs) from <i>Capsicum chinense</i> seeds (UENF 1751 accession). Fractions rich in LTPs were obtained via ion exchange chromatography and subsequently purified via reverse-phase chromatography in an HPLC system. Therefore, two fractions were revealed: C1 (the nonretained fraction) and C2 (the retained fraction in ion-exchange chromatography). Fraction C1 was subjected to reverse-phase chromatography via a C18 column on an HPLC system, and ten fractions were obtained (P1–P10), all of which significantly inhibited the growth of <i>Candida albicans</i>, except for P4 and P9. The viability analysis of the active fractions at a concentration of 100 µg.mL^-1 against <i>C. albicans</i> revealed that they did not exhibit fungicidal activity but rather exhibited fungistatic activity. The peptide is considered fungicidal when it results in the total loss of viable yeast cells, that is, when it causes the complete death of the fungi. When the substance only inhibits cell growth, but does not eliminate them completely, the effect is classified as fungistatic. Fractions P3, P4, P7, and P10 inhibited <i>Tenebrio molitor</i> larvae α-amylase. The P10 fraction presented protein bands in its electrophoretic profile with a molecular mass between 6.5 kDa and 14.2 kDa and reacted positively to an antibody produced against a protein from the LTP family bywestern blotting. The results of the analysis of amino acid residues from the P10 fraction revealed similarity between type I LTPs and type II LTPs. The ultrastructural aspects of <i>C. albicans</i> cells exposed to the P10 fraction were evaluated via transmission electron microscopy (TEM), with significant differences in their morphology being evident compared with those of the control. In summary, our results demonstrated the presence of LTPs in <i>C. chinense</i> seeds with inhibitory effects on the growth of yeasts of the genus <i>Candida</i>, which exhibited fungistatic effects and structural changes in <i>C. albicans</i> cells, in addition to exhibiting inhibitory effects on the larval insect <i>T. molitor</i> α-amylase.</p></div>","PeriodicalId":793,"journal":{"name":"The Protein Journal","volume":"44 2","pages":"201 - 212"},"PeriodicalIF":1.9,"publicationDate":"2025-02-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143384623","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Therapeutic Potential of FTO Demethylase in Metabolism and Disease Pathways","authors":"Chaitanya Sree Somala,&nbsp;Selvaraj Sathyapriya,&nbsp;Nagaraj Bharathkumar,&nbsp;Thirunavukarasou Anand,&nbsp;Damal Chandrasekar Mathangi,&nbsp;Konda Mani Saravanan","doi":"10.1007/s10930-025-10250-3","DOIUrl":"10.1007/s10930-025-10250-3","url":null,"abstract":"<div><p>The crucial involvement of the Fat Mass and Obesity-associated (FTO) protein in both metabolic and non-metabolic diseases has been documented since its discovery. This enzyme, known as FTO, is a demethylase that belongs to the 2-oxoglutarate-dependent nucleic acid demethylases. Its primary function is to target N6-methyladenosine (m⁶A) in RNA, which is crucial in regulating RNA stability, processing, and expression. This review facilitates understanding the FTO gene variations linked to Body Mass Index (BMI) and obesity, resulting in increased vulnerability to type 2 diabetes. While prior reviews have already discussed the link between FTO and BMI and its impact on type 2 diabetes, the current review additionally examines the emerging evidence suggesting a direct influence of the FTO gene on metabolism. Additionally, the paper discusses the alternative role of FTO and emphasizes the endophenotypes in neurological circuits and the demethylase function of FTO in neurodegenerative disorders. The review further examines the impact of FTO on several physiological systems and emphasizes the need to study FTO as a potential multitarget for future research and therapies.</p></div>","PeriodicalId":793,"journal":{"name":"The Protein Journal","volume":"44 1","pages":"21 - 34"},"PeriodicalIF":1.9,"publicationDate":"2025-02-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143375104","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Low-dose Bee Venom as a Potential Therapeutic Agent Against Human Chronic Myeloid Leukaemia Cells","authors":"Hamza Halici,&nbsp;Harun Un,&nbsp;Saffet Celik,&nbsp;Zeynep Karakoy,&nbsp;Zafer Bayraktutan,&nbsp;Can Ozlu,&nbsp;Elif Cadirci,&nbsp;Zekai Halici,&nbsp;Alptug Atila,&nbsp;Filiz Mercantepe","doi":"10.1007/s10930-025-10251-2","DOIUrl":"10.1007/s10930-025-10251-2","url":null,"abstract":"<div><p>Bee venom is secreted by a gland in the abdominal cavity of bees. The venom, especially that of honeybees, contains certain enzymes and peptides that, when administered in high doses, are effective against various diseases. Peptides such as melittin and phospholipase A₂ can target various cancer cells. In this study, we investigated the antiproliferative effects of administering low-dose bee venom in K-562 chronic myeloid leukaemia cells. Our proteomic study revealed regional variation of the content of bee venom and high levels of melittin, apamin and secapin, as well as phospholipase A₂ and hyaluronidase. In addition, eight new, previously unidentified proteins were identified. The effects of bee venom on cell viability and drug–cell interaction were investigated at 24, 48 and 72 h. According to the MTT (3-(4,5-Dimethylthiazol-2-yl)-2,5-Diphenyltetrazolium Bromide) results, the bee venom decreased K-562 cell viability dose-dependently at all time points. Cell viability decreased 48 and 72 h after bee venom administration but increased in the control group left untreated for 72 h. The inhibition percentages for the highest bee venom concentration (0.4 µM) at 24, 48 and 72 h were 55%, 80% and 92%, respectively. The cell–drug interactions indicated that the cell surfaces, which were smooth and clear before drug application, gradually deteriorated and started to shrink after the application. In conclusion, at increasing doses, bee venom was found to have a strong antiproliferative effect in K-562 chronic myeloid leukaemia cell lines.</p></div>","PeriodicalId":793,"journal":{"name":"The Protein Journal","volume":"44 3","pages":"297 - 307"},"PeriodicalIF":1.4,"publicationDate":"2025-02-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143384625","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}