Protein and Peptide Letters最新文献

{"title":"Unveiling the Potential Role of Hesperetin and Emodin as a Combination Therapy to Inhibit the Pancreatic Cancer Progression against the C-Met Gene.","authors":"Rangaraj Kaviyaprabha, Thandaserry Vasudevan Miji, Puthupparambil Shaji Sreelakshmi, Sridhar Muthusami, Palanisamy Arulselvan, Muruganantham Bharathi","doi":"10.2174/0109298665363165250225100109","DOIUrl":"10.2174/0109298665363165250225100109","url":null,"abstract":"<p><strong>Background: </strong>Pancreatic adenocarcinoma (PAAD) is one of the most prevalent cancers, and it has high death rates. Only 10% of PAAD patients can survive until 5 years. Hence, the improvement of survival rate of the patients should be improved.</p><p><strong>Aim: </strong>The present study used a computational approach to identify novel biomarkers and potentially effective small drug-like molecules in PAAD.</p><p><strong>Objective: </strong>The objective of this study was to identify the Differentially Expressed Genes (DEGs) and survival rate affecting genes (SDEGs) to single out the specific gene responsible for pancreatic cancer and predict the efficacy of interactions with hesperetin and emodin. Further, another objective was to validate the predicted efficacies using an MTT assay.</p><p><strong>Methods: </strong>The GEPIA2 database was used to analyze the TCGA-PAAD dataset and identify DEGs and SDEGs. Venn identified the commonly scattered genes between the DEGs and SDEGs. Network Analyst v3.0, CytoScape v3.10.1, and cytoHubbawere used to construct protein-protein interactions (PPI) network and identifying hub genes which were described as target proteins. The Protein Data Bank (PDB) and PubChem were utilized to obtain the PDB structure of the target proteins and 13 phytocompounds in SDF format. Molecular docking studies were carried out and visualized by utilizing Autodock vina and Discovery Studio Visualizer v19.1.0.1828. The cytotoxicity was measured in the MiaPaCa-2 cell line after being treated with hesperetin and emodin.</p><p><strong>Results: </strong>A total of 9219 Differentially Expressed Genes (DEGs) from the TCGA-PAAD dataset were identified. Among them, 8740 and 479 genes were up and down-regulated with the statistical significance of P ≤ 0.05, respectively. Likely, 500 most survival rate affecting genes (SDEGs) in PAAD patients with a statistical significance of P ≤ 0.05 were identified. The common 137 genes were identified between these obtained DEGs and SDEGs. The survival heat map was delineated for the predicted 137 common genes. Ninety-six genes were identified as the most hazardous genes (highlighted in red). After that, the network was constructed by using PPI for the most hazardous 96 genes. From the constructed PPI network, the highly interacted top 10 genes were identified. The survival analysis was carried out to identify the most hazardous genes and revealed that all the identified genes significantly reduced the survival rate of the patients affected by PAAD. From that, high survival affecting 5 genes, such as CDK1, CENPE, NCAPG, KIF20A, and c-MET, were selected for further analysis. The molecular docking studies were carried out for the identified top 5 genes, with the 13 phytocompounds reviewed previously for anti-- cancer activity. The molecular docking analysis revealed that the hesperetin (binding affinity (BA) = -8.0 kcal/mol; Root mean square deviation (RMSD) = 2.012 Å) and emodin (BA = -8.6 k","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":"280-298"},"PeriodicalIF":1.1,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143701385","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":"Inhibition of Canonical Wnt Signaling in Renal Cell Carcinoma Bone Metastasis: An Immunohistochemical Analysis of DKK1 and LRP5 Expression.","authors":"Zixiong Huang, Yiqing Du, Huaqi Yin, Gongwei Wang, Tao Xu","doi":"10.2174/0109298665357331250416081850","DOIUrl":"10.2174/0109298665357331250416081850","url":null,"abstract":"<p><strong>Background and objective: </strong>Canonical Wnt (Wnt/β-catenin) signaling maintains bone homeostasis by promoting osteoblastic activities. The inhibitory factor, Dickkopf-1 (DKK1), enhances bone resorption in malignant diseases. Low-density lipoprotein-related protein (LRP) 5 is antagonized by DKK1. This study aimed to investigate the expression of DKK1 and LRP5 in renal cell carcinoma bone metastasis (RCC-BM).</p><p><strong>Methods: </strong>RCC-BM patients with paired samples of primary and metastatic lesions were selected for the study (RCC-BM group). RCC patients without any metastasis served as the control group (RCC-only group). Immunohistochemical staining with monoclonal anti-DKK1 and polyclonal anti- LRP5 antibody was conducted on paraffin-embedded slides. The staining results were recorded using scoring according to staining intensity in the renal tissue adjacent to the tumor, primary RCC lesions, and RCC-BM lesions.</p><p><strong>Results: </strong>DKK1 was differently expressed among normal renal tissues, primary RCC, and RCC- BM tissues (p<0.001). The DKK1 expression in primary RCC was significantly lower than that in normal renal tissues (p<0.001) without a difference between the RCC-BM and RCC-only groups. DKK1 expression in bone metastasis was significantly higher than that in primary tumors (p<0.001). For RCC-BM patients, the expression of LRP5 in the primary tumor was significantly lower than that in adjacent renal tissues (p<0.01). The tendency of lower expression was found in primary RCC from RCC-BM patients compared to RCC without metastasis (p=0.073).</p><p><strong>Conclusion: </strong>A \"rebound\" pattern of DKK1 expression in bone metastasis lesions and the decreasing LRP5 expression in primary lesions of RCC-BM patients suggested that Wnt/β-catenin signaling was inhibited in RCC-BM. The overexpression of DKK1 and reduced expression of LRP5 suggest that these markers may be useful for the early prediction of RCC-BM.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":"327-334"},"PeriodicalIF":1.1,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144028841","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":"Molecular Cloning and Expression of Cryptocyanin Gene Isolated from an Indian Variety of <i>Scylla olivacea</i>.","authors":"Simran Mann, Chittibabu Shanthi, Manu Asthana","doi":"10.2174/0109298665387863250506105601","DOIUrl":"10.2174/0109298665387863250506105601","url":null,"abstract":"<p><strong>Background: </strong>Molting and reproduction play vital roles in the life cycle of brachyuran crabs, and these two processes are closely interconnected. A key player in the molting cycle is cryptocyanin, which is similar to hemocyanin in sequence, size, and structure. Hemocyanin is a copper-containing oxygen-binding protein, while cryptocyanin is a copper-free protein that lacks oxygen-binding capacity.</p><p><strong>Objective: </strong>The goal of the study was to carry out the isolation, cloning, and expression of the partial cryptocyanin gene from the Indian variety of <i>Scylla olivacea</i>.</p><p><strong>Methods: </strong>The partial cryptocyanin gene was isolated from the hemocytes of the <i>S. olivacea</i> male and female crabs by qPCR for comparative expression analysis of the cryptocyanin gene.</p><p><strong>Results: </strong>We successfully amplified, cloned, and expressed a 519 bp partial cDNA encoding cryptocyanin from the Indian variety of<i> Scylla olivacea</i>, within the pRSET-B vector.</p><p><strong>Discussion: </strong>In this study, we conducted a comprehensive analysis of cryptocyanin expression in male and female crabs during the intermolt stage. Our findings revealed Cq values of 28.97 for males and 33.68 for females, highlighting a significantly lower abundance of cryptocyanin protein in female crabs.</p><p><strong>Conclusion: </strong>Our study showed that crustacean cDNA can be effectively expressed in bacterial vectors, and clones were stable for up to 6 months at -80oC. Real-time data showed a significant difference in cryptocyanin levels between male and female crabs. This finding highlights the need for further research with a larger sample size for better understanding.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":"368-375"},"PeriodicalIF":1.1,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144143106","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":"MARVELD1 Promotes the Invasiveness in Pancreatic Adenocarcinoma through the Activation of Epithelial-to-Mesenchymal Transition.","authors":"Xianwei Luo, Zhenming Gao","doi":"10.2174/0109298665359781250114055525","DOIUrl":"10.2174/0109298665359781250114055525","url":null,"abstract":"<p><strong>Background: </strong>MARVEL domain-containing 1 (MARVELD1) has been implicated in the progression of several cancers, but its role in pancreatic adenocarcinoma (PAAD) remains poorly understood.</p><p><strong>Methods: </strong>RNA-seq data from the TCGA-PAAD and GTEx-Pancreas cohorts were analyzed to assess MARVELD1 expression. Stable MARVELD1 knockdown and overexpression were conducted in BxPC3 and PANC-1 cells. Cell viability, proliferation, migration, and invasion were evaluated using functional assays, and western blotting was employed to examine EMT-associated protein levels, including Vimentin, MMP2, MMP9, and E-cadherin. Differentially expressed genes (DEGs) between MARVELD1-high and MARVELD1-low groups were identified, and pathway enrichment analyses were performed.</p><p><strong>Results: </strong>We observed a significant increase of MARVELD1 in PAAD patient samples, with elevated MARVELD1 levels correlating with poor clinical survival. Knockdown of MARVELD1 in PAAD cells remarkably decreased cell proliferation and colony formation, while overexpression of MARVELD1 enhanced these properties. Moreover, simulated cell invasion and migration assay further suggested that MARVELD1 might contribute to PAAD cell aggressiveness. Mechanistically, MARVELD1 promoted tumor cell migration and invasion through the activation of Vimentin, MMP2, and MMP9 protein while suppressing E-cadherin. Bioinformatics analysis revealed that MARVELD1-high samples were enriched in EMT-related pathways, including TGF-β receptor signaling, actin cytoskeleton regulation, and cell adhesion.</p><p><strong>Conclusion: </strong>Taken together, our study highlights the roles of MARVELD1 in promoting tumor cell proliferation and invasion, suggesting its potential application as a prognostic and diagnostic biomarker for PAAD in the clinical context.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":"224-233"},"PeriodicalIF":1.0,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143024413","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":"Design, Expression, and Purification of a Fusion Enzyme Containing Terminal Deoxynucleotidyl Transferase from <i>B. bovis</i> and DNA-Binding Proteins from <i>E. coli</i>.","authors":"Antos Sachanka, Veronika Shchur, Yaraslau Dzichenka, Aleksei Yantsevich","doi":"10.2174/0109298665372636250504084653","DOIUrl":"10.2174/0109298665372636250504084653","url":null,"abstract":"<p><strong>Background: </strong>Gene fusion techniques have yielded promising results in the fusion of thermostable polymerases (Taq and Pfu) with single-stranded and double-stranded DNA-binding proteins. Constructing a terminal deoxynucleotidyl transferase (TdT) fusion enzyme with DNAbinding protein domains can enhance thermostability and broaden the enzyme's application field. This makes it a promising candidate for cost-effective <i>de novo</i> DNA synthesis and a more effective tool for demonstrating apoptosis and detecting viral DNA/RNA.</p><p><strong>Methods: </strong>The design of fusion proteins was based on molecular dynamics and homology modeling. Native and fusion proteins were isolated using affinity chromatography on HisTrap HP. Thermostability was assessed through differential scanning fluorimetry and dynamic light scattering. HPLC analysis was conducted to evaluate enzyme activity.</p><p><strong>Results: </strong>According to the <i>in silico</i> predictions of the fusion protein structure, a homotetramer was formed. The expressed fusion proteins were successfully purified under native conditions, similar to TdT. The total yields of the studied proteins were 130 mg/L for single-stranded binding protein from <i>E. coli</i> (EcSSB), 5 mg/L for TdT, 9 mg/L for TdT_L1_EcSSB, and 7 mg/L for TdT_L2_EcSSB. The measured radius of TdT (3.5 nm) was found to be consistent with a monomeric structure; however, the fusion proteins were expected to form a homotetramer. Additionally, fusion with EcSSB was found to prevent aggregation, which positively affected the thermal stability of the fusion protein. Instead of elongating the substrate by adding nucleotides, the fusion enzyme removed a nucleotide, specifically TTP, from the 3'-end of the DNA strand.</p><p><strong>Conclusion: </strong>The fusion of TdT with EcSSB resulted in increased thermal stability and a reduced ability to add nucleotides to the substrate.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":"353-367"},"PeriodicalIF":1.1,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144142991","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":"Targeting APE1: Advancements in the Diagnosis and Treatment of Tumors.","authors":"Minghui Hu, Yingyu Zhang, Pin Zhang, Kangbo Liu, Mengxin Zhang, Lifeng Li, Zhidan Yu, Xianwei Zhang, Wancun Zhang, Ying Xu","doi":"10.2174/0109298665338519241114103223","DOIUrl":"10.2174/0109298665338519241114103223","url":null,"abstract":"<p><p>With the emergence of the precision medicine era, targeting specific proteins has emerged as a pivotal breakthrough in tumor diagnosis and treatment. Apurinic/apyrimidinic Endonuclease 1 (APE1) is a multifunctional protein that plays a crucial role in DNA repair and cellular redox regulation. This article comprehensively explores the fundamental mechanisms of APE1 as a multifunctional enzyme in biology, with particular emphasis on its potential significance in disease diagnosis and strategies for tumor treatment. Firstly, this article meticulously analyzes the intricate biological functions of APE1 at a molecular level, establishing a solid theoretical foundation for subsequent research endeavors. In terms of diagnostic applications, the presence of APE1 can be detected in patient serum samples, biopsy tissues, and through cellular in situ testing. The precise detection methods enable changes in APE1 levels to serve as reliable biomarkers for predicting tumor occurrence, progression, and patient prognosis. Moreover, this article focuses on elucidating the potential role of APE1 in tumor treatment by exploring various inhibitors, including nucleic acid-based inhibitors and small molecule drug inhibitors categories, and revealing their unique advantages in disrupting DNA repair function and modulating oxidative-reduction activity. Finally, the article provides an outlook on future research directions for APE1 while acknowledging major technical difficulties and clinical challenges that need to be overcome despite its immense potential as a target for tumor therapy.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":"18-33"},"PeriodicalIF":1.0,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142795056","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":"Anti-Cancer Bioactive Peptide Induces Apoptosis in Gastric Cancer Cells through TP53 Signaling Cascade.","authors":"Qimuge Suyila, Xian Li, Xiulan Su","doi":"10.2174/0109298665350654250111144722","DOIUrl":"10.2174/0109298665350654250111144722","url":null,"abstract":"<p><strong>Introduction: </strong>Gastric cancer has emerged as one of the major diseases threatening human health. Our previous studies indicated that the anti-cancer bioactive peptide (ACBP) inhibits the initiation and progression of gastric cancer through apoptosis and cell cycle arrest, yet the mechanisms remain unclear. To elucidate the relationships between the effects of ACBP and the levels of cell differentiation, as well as the functional mechanisms of ACBP, we conducted a study using three human gastric cancer cell lines: NCI-N87, MGC-803, and another unspecified line.</p><p><strong>Methods: </strong>We investigated the impact of ACBP on the survival and morphology of these cancer cell lines, examined apoptosis and cell cycle progression, and detected the expression of TP53, TP63, and TP73 in cancer cells, as well as the expression of Bax, PUMA, and Mcl-1 in a xenograft mouse model. ACBP inhibited the proliferation of all three cancer cell lines in a dose-dependent manner, similar to the positive control and 5-fluorouracil (5-FU). The effect of ACBP correlated with the degree of differentiation of the cancer cells; the lower the differentiation degree, the stronger the inhibitory effect.</p><p><strong>Results: </strong>After ACBP treatment, the expression of TP53, TP63, and TP73 increased in all cell lines. In the xenograft mouse model, ACBP inhibited the growth of MGC-803 cells in vivo. The apoptotic-related genes Bax and PUMA were upregulated, while Mcl-1 was downregulated. ACBP inhibited tumor cell growth by inducing apoptosis through the TP53 signaling cascade, upregulating TP53, TP63, and TP73 and their downstream apoptosis-promoting genes Bax and PUMA while downregulating the anti-apoptotic gene Mcl-1.</p><p><strong>Conclusion: </strong>Notably, after ACBP treatment, Mcl-1 expression was significantly reduced in the tumor tissue of the xenograft model, indicating that ACBP induced apoptosis through the TP53 signaling cascade. This project provides a scientific basis for exploring the antitumor mechanism of ACBP in gastric cancer therapy.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":"194-205"},"PeriodicalIF":1.0,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143415054","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":"Molecular Interactions of the Antimicrobial Peptide Tritrpticin with Mixed Nanoaggregates: A Fluorescence Spectroscopy Study.","authors":"Kaio César Antunes Rocha, Maria Carolina Oliveira de Arruda Brasil, Eduardo Maffud Cilli, Luiz Carlos Salay","doi":"10.2174/0109298665359223241226091327","DOIUrl":"10.2174/0109298665359223241226091327","url":null,"abstract":"<p><strong>Introduction: </strong>Tritrpticin (TRP3) is a peptide belonging to the cathelicidin family and has a broad spectrum of antimicrobial activity. However, this class of biomolecules can be easily degraded in the body, making it necessary to use an efficient transport system. The ability to form stable nanostructures from the interaction of glycyrrhizin saponin with the pluronic polymer F127 was demonstrated, forming mixed biopolymeric micelles, highly promising as drug carriers.</p><p><strong>Objective: </strong>The present work sought to understand the physicochemical interaction of the antimicrobial peptide TRP3 with the mixed polymeric micelle made from pluronic F127 and the saponin glycyrrhizin.</p><p><strong>Methods: </strong>The interaction of tritrpticin with mixed nanostructured micelles was evaluated through fluorescence spectroscopy and fluorescence quenching with acrylamide. The experiments were performed at room temperature (25 ± 1°C), adopting an excitation wavelength set to 280 nm and emission between 300 and 500 nm, with a slit of 5 nm.</p><p><strong>Results: </strong>The interaction of the cationic peptide tritrpticin with the mixed biopolymeric micelles was observed through the blue shift of the fluorescence emission to shorter wavelengths, proving the change of tryptophan to a more hydrophobic environment. Through the fluorescence suppression technique, it was possible to indicate the location of the peptide in the mixed micelles, proving tritrpticin to be partially inserted inside them.</p><p><strong>Conclusion: </strong>It was concluded that tritrpticin interacted with mixed nanostructured micelles, forming a promising system for biotechnological applications.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":"152-160"},"PeriodicalIF":1.0,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143060508","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":"Diminazene Aceturate (DIZE) Ameliorates Hypertension and Induces Anxiolytic- and Antidepressant-like Effects in TGR(mRen2)27.","authors":"Laura Amado Costa, Flavio A G Mourao, Natalia Alenina, Michael Bader, Maria Jose Campagnole-Santos, Lucas M Kangussu","doi":"10.2174/0109298665357730250213050214","DOIUrl":"10.2174/0109298665357730250213050214","url":null,"abstract":"<p><strong>Introduction: </strong>Diminazene aceturate (DIZE) was described as an angiotensin-converting enzyme 2 (ACE2) activator. ACE2/Angiotensin-(1-7)/Mas receptor axis presents protective actions on cardiovascular diseases and plays an important modulatory role in the neurobiology of mood and anxiety disorders.</p><p><strong>Objectives: </strong>To evaluate the effects of chronic intracerebroventricular (ICV) treatment with DIZE on blood pressure, anxiety- and depression-like behaviors in hypertensive transgenic (mRen2)27 rats (TGR).</p><p><strong>Methods: </strong>Male TGR and Sprague-Dawley rats (10-12 weeks old) were subjected to chronic ICV infusion of DIZE (1.0 μg/h for 7 days). Blood pressure and heart rate were measured by tail plethysmography and anxiety- and depression-like behaviors were evaluated through elevated plus maze, marble burying and forced swim tests, respectively.</p><p><strong>Results: </strong>Treatment with DIZE induced a significant reduction in mean arterial pressure in both TGR and SD rats. A decrease in heart rate was only observed in the hypertensive animals. Additionally, treatment with DIZE attenuated the anxiety- and depression-like behaviors that were observed in TGR.</p><p><strong>Conclusion: </strong>DIZE has central anti-hypertensive, anxiolytic, and anti-depressive effects.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":"243-252"},"PeriodicalIF":1.1,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143493446","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":"Cell-Free Expression of HPV16 Minor Capsid Protein L2 and Its Interaction with S100A10.","authors":"Wenqi Jiang, Lian Wu, Xiangchun Shen, Qingshan Bill Fu","doi":"10.2174/0109298665390494250513110604","DOIUrl":"10.2174/0109298665390494250513110604","url":null,"abstract":"<p><strong>Background: </strong>Human papillomavirus type 16 (HPV16) is implicated in various malignancies. The virus enters host cells through endocytosis, during which the minor capsid protein L2 interacts with the S100A10 subunit of the annexin A2 heterotetramer (A2t) on the host cell membrane. This interaction is critical for facilitating HPV entry and subsequent infection of human cells. Therefore, examining the interaction between the L2 protein and S100A10 is crucial for advancing our understanding of the mechanisms by which HPV16 infiltrates cells.</p><p><strong>Objective: </strong>The cell-free expression (CFE) system was investigated for L2 purification. The structure of L2 was characterized and its interaction with S100A10 was explored.</p><p><strong>Methods: </strong>The L2 protein was expressed using a CFE expression system, and its expression was verified via Western blotting. L2 was further purified through size-exclusion chromatography (SEC), and its structural features were preliminarily assessed using transmission electron microscopy (TEM) and circular dichroism (CD) spectroscopy. Additionally, surface plasmon resonance (SPR) was employed to analyze the interaction between L2 and S100A10.</p><p><strong>Results: </strong>Western blotting confirmed the successful expression of L2. TEM and CD provided preliminary structural observations of L2, and SPR measurements yielded precise kinetic parameters for the interaction between L2 and S100A10.</p><p><strong>Conclusion: </strong>In this study, we successfully expressed the HPV16 L2 protein using a cell-free protein expression system. Preliminary structural analysis using TEM and CD revealed key structural features of L2. Furthermore, SPR analysis provided detailed kinetic parameters for its interaction with S100A10. These findings provide more details on understanding L2's structural features, with broader implications for antipathogen studies.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":"376-386"},"PeriodicalIF":1.1,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144142985","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}