Protein and Peptide Letters最新文献

{"title":"Evaluation of Cytotoxicity and Antimicrobial Activity of Experimental Composites Containing Chitosan-Silver Oxide Particles Against Two Main Pathogenic Bacteria in Periodontal Disease.","authors":"Nahid Nasrabadi, Navid Ramezanian, Parisa Ghorbanian, Ali Forouzanfar, Hamideh Sadat Mohammadipour","doi":"10.2174/0109298665240242231016103321","DOIUrl":"10.2174/0109298665240242231016103321","url":null,"abstract":"<p><strong>Introduction: </strong>Bacterial biofilm is known as the main cause of periodontal disease. Generally, the anaerobic Gram-negative, such as <i>Porphyromonas gingivalis</i> and Fusobacterium nucleatum, are considered the most identified bacteria.</p><p><strong>Objective: </strong>This study aimed to investigate the antimicrobial effect and cytotoxicity of two experimental composites containing chitosan-silver oxide (CH-Ag₂O) particles.</p><p><strong>Materials and methods: </strong>Four experimental groups, including Ag2O and CH, along with two composites of CH-Ag₂O 20 and CH-Ag₂O 60 mg, were prepared. Antimicrobial activity was performed against <i>Porphyromonas gingivalis</i> (ATCC#33277) and Fusobacterium nucleatum (ATCC#25586) using the agar dilution method. Moreover, the cytotoxicity assay was performed on human gingival fibroblasts (HGF) by the use of the MTT method. The obtained data were analyzed with descriptive methods, one-way ANOVA, and Tukey's LSD tests.</p><p><strong>Results: </strong>The antibacterial activity of both composites was higher than both CH and Ag₂O, and the greatest antibacterial properties were presented in CH-Ag₂O 60. In all three measurements (24, 48, and 72 h), the greatest cytotoxicity was seen in Ag₂O, followed by CH, CH-Ag₂O 20, and CHAg₂O 60 in descending order, respectively. The cytotoxicity of these components was related to the concentration and not to the time of exposure. The results showed that Ag₂O in 3.7 and 7.5 μg/ml concentrations and CH-containing groups in 250 and 500 μg/ml were toxic to the cultured HGF.</p><p><strong>Conclusion: </strong>The experimental composite containing CH-Ag₂O 60 showed the greatest antibacterial properties against two periodontal pathogens evaluated. In order to clarify the clinical significance of composite cytotoxicity, further clinical studies are necessary.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":"97-106"},"PeriodicalIF":1.6,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71426296","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":"The GA-Hecate Peptide inhibits the ZIKV Replicative Cycle in Different Steps and can Inhibit the Flavivirus NS2B-NS3 Protease after Cell Infection.","authors":"Paulo Ricardo da Silva Sanches, João Caldana Elias de Campos Faria, Cíntia Bittar, Hugo Alexandre Siqueira Guberovich Olivieri, Nathalya Cristina de Moraes Roso Mesquita, Gabriela Dias Noske, Andre Schutzer de Godoy, Glaucius Oliva, Paula Rahal, Eduardo Maffud Cilli","doi":"10.2174/0109298665308871240703090408","DOIUrl":"10.2174/0109298665308871240703090408","url":null,"abstract":"<p><strong>Background: </strong>Peptide drugs are advantageous because they are subject to rational design and exhibit highly diverse structures and broad biological activities. The NS2B-NS3 protein is a particularly promising flavivirus therapeutic target, with extensive research on the development of inhibitors as therapeutic candidates, and was used as a model in this work to determine the mechanism by which GA-Hecate inhibits ZIKV replication.</p><p><strong>Objective: </strong>The present study aimed to evaluate the potential of GA-Hecate, a new antiviral developed by our group, against the Brazilian Zika virus and to evaluate the mechanism of action of this compound on the flavivirus NS2B-NS3 protein.</p><p><strong>Methods: </strong>Solid-phase peptide Synthesis, High-Performance Liquid Chromatography, and Mass Spectrometry were used to obtain, purify, and characterize the synthesized compound. Real-time and enzymatic assays were used to determine the antiviral potential of GA-Hecate against ZIKV.</p><p><strong>Results: </strong>The RT-qPCR results showed that GA-Hecate decreased the number of ZIKV RNA copies in the virucidal, pre-treatment, and post-entry assays, with 5- to 6-fold fewer RNA copies at the higher nontoxic concentration in Vero cells (HNTC: 10 μM) than in the control cells. Enzymatic and kinetic assays indicated that GA-Hecate acts as a competitive ZIKV NS2B-NS3 protease inhibitor with an IC₅₀ of 32 nM and has activity against the yellow fever virus protease.</p><p><strong>Conclusion: </strong>The results highlight the antiviral potential of the GA-Hecate bioconjugate and open the door for the development of new antivirals.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":"532-543"},"PeriodicalIF":1.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141748948","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":"Exploring the Cell Wall and Secretory Proteins of <i>Mycobacterium leprae</i> as Biomarkers.","authors":"Sakshi Singh, Devesh Sharma, Sakshi Gautam, Mamta Arora, Deepa Bisht","doi":"10.2174/0109298665267993231026114709","DOIUrl":"10.2174/0109298665267993231026114709","url":null,"abstract":"<p><p>The bacterial cell wall is composed of a wide variety of intricate proteins in addition to lipids, glycolipids, and polymers. Given the diversity of cell wall proteins among bacterial species, they are a feasible target for biomarker identification and characterization in clinical research and diagnosis of the disease. The slow growth rate of <i>Mycobacterium leprae</i> poses a major hurdle in the accurate diagnosis of leprosy before the onset of peripheral neuropathy. The use of biomarker- based diagnostic methods can help in preventing the spread and manifestation of leprosy. Despite many advances in research methods and techniques, there remains a knowledge gap regarding the cell wall proteomes of <i>M. leprae</i> that can be used as biomarkers. The cell wall and secretory proteins of <i>M. leprae</i> are the major focus of this review article. This article enfolds the characteristics and functions of <i>M. leprae</i> cell wall proteins and gives an insight into those cell wall proteins that are yet to be established as biomarkers. Tools and techniques used in cell wall extraction and biomarker identification can also be explored in this article.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":"11-24"},"PeriodicalIF":1.6,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"92156254","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":"Improving Photocleavage Efficiency of Photocleavable Protein for Antimicrobial Peptide Histatin 1 Expression.","authors":"Nana Zhou, Tai An, Yuan Zhang, Guomiao Zhao, Chao Wei, Xuemei Shen, Fan Li, Xiaoyan Wang","doi":"10.2174/0109298665276722231212053009","DOIUrl":"10.2174/0109298665276722231212053009","url":null,"abstract":"<p><strong>Background: </strong>Antimicrobial peptides (AMPs) are promising alternative agents for antibiotics to overcome antibiotic resistance problems. But, it is difficult to produce large-scale antimicrobial research due to the toxicity towards expression hosts or degradation by peptidases in the host. Therefore, heterologous recombinant expression of antimicrobial peptides has always been a challenging issue.</p><p><strong>Objectives: </strong>To overcome toxicity to the expression host and low expression level, a new photocleavable protein fusion expression method for antimicrobial peptides is provided.3 Methods: Through directed evolution and high throughput screening, a photocleavable protein mutant R6-2-6-4 with a higher photocleavage efficiency was obtained. The DNA coding sequence of antimicrobial peptide Histatin 1 was fused within the sequence of R6-2-6-4 gene. The fusion gene was successfully expressed in <i>Escherichia coli</i> expression system.</p><p><strong>Results: </strong>Antimicrobial peptide Histatin 1 could be successfully expressed and purified by fusing within PhoCl mutant R6-2-6-4. The antimicrobial activity was rarely affected, and the MIC value was 33 ug/mL, which was basically equivalent to 32 ug/mL of the chemically synthesized Histatin 1. After amplification in a 5 L fermenter, the expression of PhoCl mutant (R6-2-6-4)-Histatin1 improved up to 87.6 mg/L in fermenter, and Histatin1 obtained by photocleavage also could up to 11 mg/L. The prepared Histatin1 powder remained stable when stored at 4oC for up to 4 months without any degradation. In addition, the expression and photocleavage of β -Defensin105 and Lysostaphin verified the certain universality of the PhoCl mutant fusion expression system.</p><p><strong>Conclusion: </strong>Antimicrobial peptides Histatin 1, β -Defensin 105 and Lysostaphin were successfully expressed and purified by photocleavable protein mutant. This may provide a novel strategy to express and purify antimicrobial peptides in the <i>Escherichia coli</i> expression system.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":"141-152"},"PeriodicalIF":1.6,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139513364","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":"Characterization of Luciferase from <i>Photorhabdus kayaii</i> and its Application for <i>In vivo</i> Imaging Studies in Mice.","authors":"Shirin Tarahomjoo, Laleh Ebrahimi, Fatemeh Valishahavaz, Maryam Taghdiri, Reza Banihashemi","doi":"10.2174/0109298665277974240926064439","DOIUrl":"10.2174/0109298665277974240926064439","url":null,"abstract":"<p><strong>Background: </strong>Bioluminescence, or the production of light by luciferases, is the basis of a well-known reporter technology. A quick way to study the efficacy of antimicrobial drugs and vaccines is <i>in vivo</i> bioluminescence imaging (BLI). <i>Photorhabdus</i> spp. represent the only terrestrial group of bioluminescent bacteria. The luciferase obtained from <i>Photorhabdus luminescence</i> has been widely used in BLI studies. However, little information is available about the functions of luciferases obtained from other members of this genera.</p><p><strong>Objective: </strong>This study aimed to evaluate the applicability of the luciferase obtained from <i>Photorhabdus kayaii</i> for BLI studies.</p><p><strong>Methods: </strong><i>P. kayaii</i> starE, an Iranian isolate of <i>P. kayaii</i>, was cultivated on NBTA agar plates. The resulting colonies were cultured on McConkey agar to determine the bacterial phase. Bioluminescence emission was measured using a multimode reader. The luciferase genes of this bacterium were sequenced following the PCR amplification, and the corresponding amino acid sequences were determined. The luciferase tertiary structure was then obtained from the TACOS web server and compared to that of <i>P. luminescence</i> in CE software. The <i>lux</i> operon encoding the luciferase (luxA and luxB genes) and substrate synthesis complex was cloned and expressed in <i>Escherichia</i> coli BL21 (DE3) using the pBBR1MCS2_START vector. The luminescence emission during the growth was examined. Moreover, the effects of pH and sodium deoxycholate (bile salt) on bioluminescence emission were investigated. Appropriate conditions for the use of bioluminescent E. coli for BLI studies in mice were demonstrated in terms of cell numbers and injection routes.</p><p><strong>Results: </strong>The bacterium was luminescent and in phase I. Its luciferase monomers (α and β) shared 100% amino acid homology with P. kayaii M-HU2 and more than 92% with <i>P. luminescence</i>. Tertiary structures of the luciferase monomers were 93%- 95% identical to those of P. luminescence. The lux operon was expressed in E. coli, and the maximum bioluminescence signal was observed during the decelerating phase of growth. The bioluminescence at different pH values correlated with the cell survival. The luminescence was emitted by cells exposed to the bile salt. A strong bioluminescent signal was emitted from mice after subcutaneous injection of bioluminescent <i>E. coli</i> at 10⁷ CFU. However, no signals were emitted from mice that were administered the same cell number via intraperitoneal injection. A 2.5-fold increase in the cell number resulted in bioluminescence detection in the abdomen of mice after intraperitoneal injection and a 3.22-fold increase in signal intensity after subcutaneous injection.</p><p><strong>Conclusion: </strong>These results demonstrated the usefulness of P. kayaii luciferase for BLI studies.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":"806-817"},"PeriodicalIF":1.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142506627","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":"A Conserved Tryptophan (Trp10) at the Hydrophobic Core Modulates the Stability and Inhibitory Activity of Potato I Type Inhibitors.","authors":"Xiaodong Cui, Jiahui Shen, Jiajie Wang, Chen Li, Fang Li, Jiao Li","doi":"10.2174/0109298665333930240905111039","DOIUrl":"10.2174/0109298665333930240905111039","url":null,"abstract":"<p><strong>Background: </strong>Different inhibitor families have their own conserved three-dimensional structures, but how these structures determine whether a protein can become an inhibitor is still unknown. The buckwheat trypsin inhibitor (BTI) pertains to the Potato I type inhibitor family, which is a simple and essential bio-molecule that serves as a model for the investigation of protease-inhibitor interaction.</p><p><strong>Objective: </strong>To study the effects of mutations at Trp10 and Ile25 in the hydrophobic cavity (scaffold) of rBTI on its inhibitory activity and stability.</p><p><strong>Methods: </strong>Site-directed mutagenesis and molecular modeling were performed using the sequence of BTI. The hydrogen bonds formed by all amino acids and conformational differences of Trp53 were analyzed in the tertiary structures of rBTI and mutants.</p><p><strong>Results: </strong>Mutant rBTI-W10A almost completely lost its inhibitory activity (retaining 10%), while rBTI-I25A retained about 50% of its inhibitory activity. Both rBTI-W10A and rBTI-I25A could be degraded by trypsin. The hydrogen bond analysis results showed that mutating Trp10 or Ile25 weakened the specific cohesion interactions in the hydrophobic core of rBTI, disrupting the tight hydrogen bond network in the cavity. This further led to difficulty in maintaining the binding loop conformation, ultimately causing the Trp53 to undergo conformational changes. It was also difficult for residues in the mutants to form hydrogen bonds with amino acids in bovine trypsin; thus, the mutants could not stably bind to trypsin.</p><p><strong>Conclusion: </strong>Our findings suggest that the hydrophobic core is also an important factor in the maintenance of inhibitory activity and stability of rBTI.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":"736-747"},"PeriodicalIF":1.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142352670","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":"<i>UPBEAT1</i>-ROS-POD-<i>PAL</i> System under Different Xylogenesis Scenarios in Karelian Birch <i>(Betula pendula</i> Roth var. carelica (Mercl.) Hämet-Ahti).","authors":"Kseniya Mihajlovna Nikerova, Nataliya Alekseevna Galibina, Irina Nikolaevna Sofronova, Yuliya Leonidovna Moshchenskaya, Maksim Anatol'evich Korzhenevskij, Anna Vladimirovna Klimova, Tatiana Vladimirovna Tarelkina","doi":"10.2174/0109298665291781240529044444","DOIUrl":"10.2174/0109298665291781240529044444","url":null,"abstract":"<p><strong>Background: </strong>We studied <i>UPBEAT1 (UPB1)</i> which regulated superoxide radical / hydrogen peroxide ratio together with peroxidase (POD) activity and <i>PAL</i> genes expression under different ways of apical meristem development during the xylem structural elements' formation in unique woody plants <i>B. pendula</i> var. pendula with straight-grained wood and <i>B. pendula</i> var. carelica with figured wood. The differentiation process predominanced in straight-grained wood (<i>B. pendula</i> var. <i>pendula</i>) or proliferation - in the figured wood. The investigation was conducted in the radial row (cambial zone - differentiating xylem - mature xylem) during the active cambial growth period.</p><p><strong>Objective: </strong>The study aimed to study the xylogenesis processes occurring in the 16-year-old straight-grained silver birch (<i>Betula pendula</i> Roth) and Karelian birch (<i>Betula pendula</i> Roth var. carelica (Mercl.) Hämet-Ahti) with figured wood.</p><p><strong>Methods: </strong>Hydrogen peroxide and superoxide radical contents and peroxidase activity were determined spectrophotometrically. Gene expression for <i>PAL</i> family genes and the <i>UPBEAT1</i> gene was assessed using qRT-PCR.</p><p><strong>Results: </strong>Principal component analysis has confirmed trees with straight-grained and figured wood to be different according to UPBEAT1-ROS-POD-<i>PAL</i> system functioning.</p><p><strong>Conclusion: </strong>The higher superoxide radical/hydrogen peroxide ratio in figured Karelian birch, along with <i>UPBEAT1</i> transcription factor and <i>PAL</i> genes upregulation, distinguished it from straight-grained silver birch. This metabolic picture confirmed the shift of Karelian birch xylogenesis towards proliferation processes, accompanied by ROS and phenolic compounds' flow and POD activity.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":"375-385"},"PeriodicalIF":1.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141262747","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":"Preface.","authors":"Ben M Dunn","doi":"10.2174/092986653101240120234231","DOIUrl":"10.2174/092986653101240120234231","url":null,"abstract":"","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":"31 1","pages":"2"},"PeriodicalIF":1.6,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140040194","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":"Characterization of a Novel Thermostable 7α-Hydroxysteroid Dehydrogenase.","authors":"Deshuai Lou, Yangyang Cao, Hongtao Duan, Jun Tan, Binyan Li, Yuanjun Zhou, Dong Wang","doi":"10.2174/0109298665279004231229100320","DOIUrl":"10.2174/0109298665279004231229100320","url":null,"abstract":"<p><strong>Background: </strong>7α-Hydroxysteroid dehydrogenase (7α-HSDH) plays a pivotal role in vivo in the biotransformation of secondary bile acids and has great potential in industrial biosynthesis due to its broad substrate specificity. In this study, we expressed and characterized a novel thermostable 7α-HSDH (named Sa 7α-HSDH).</p><p><strong>Methods: </strong>The DNA sequence was derived from the black bear gut microbiome metagenomic sequencing data, and the coding sequence of Sa 7α-HSDH was chemically synthesized. The heterologous expression of the enzyme was carried out using the pGEX-6p-1 vector. Subsequently, the activity of the purified enzyme was studied by measuring the absorbance change at 340 nm. Finally, the three-dimensional structure was predicted with AlphaFold2.</p><p><strong>Results: </strong>Coenzyme screening results confirmed it to be NAD(H) dependent. Substrate specificity test revealed that Sa 7α-HSDH could catalyze taurochenodeoxycholic acid (TCDCA) with catalytic efficiency (k_cat/K_m) 3.81 S-1 mM-1. The optimum temperature of Sa 7α-HSDH was measured to be 75°C, confirming that it belongs to thermophilic enzymes. Additionally, its thermostability was assessed using an accelerated stability test over 32 hours. The catalytic activity of Sa 7α-HSDH remained largely unchanged for the first 24 hours and retained over 90% of its functionality after 32 hours at 50°C. Sa 7α-HSDH exhibited maximal activity at pH 10. The effect of metal ions-K⁺, Na⁺, Mg²⁺ and Cu²⁺-on the enzymatic activity of Sa 7α-HSDH was investigated. Only Mg²⁺ was observed to enhance the enzyme's activity by 27% at a concentration of 300 mM. Neither K⁺ nor Na+ had a significant influence on activity. Only Cu²⁺ was found to reduce enzyme activity.</p><p><strong>Conclusion: </strong>We characterized the thermostable 7α-HSDH, which provides a promising biocatalyst for bioconversion of steroids at high reaction temperatures.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":"153-160"},"PeriodicalIF":1.6,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139576251","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":"Immunoproteomics: Approach to Diagnostic and Vaccine Development.","authors":"Virendra Supaji Gomase, Suchita Prabhakar Dhamane, Kiran Ramesh Kemkar, Pavan Ganpat Kakade, Abhay Dewappa Sakhare","doi":"10.2174/0109298665342261240912105111","DOIUrl":"10.2174/0109298665342261240912105111","url":null,"abstract":"<p><p>The study of large protein sets (proteomics) involved in the immunological reaction is known as immunoproteomics. The methodology of immunoproteomics plays a major role in identifying possible vaccine candidates that could protect against pathogenic infection. The study of immunogenic proteins that are expressed during the outset of infection is the focus of the crosstalk between proteomics and immune protection antigens utilizing serum. Peptide presentation by MHC provides the new 'window' into changes that occur in the cell. Thus, there is strong, intense pressure on the pathogen that has been mutated in such an unusual manner that it can bypass the MHC peptide presentation by the MHC molecule. The pathogen's ability to evade the immune system is strongly restricted by the two unique distinct properties of MHC molecules, i.e., polygenic and polymorphic properties. MHC-I restriction epitope identification has traditionally been accomplished using genetic motif prediction. The study of immune system proteins and their interactions is the main emphasis of the specialist field of immunoproteomics within proteomics. Methodologies include mass spectrometry (MS), SRM assay, MALDI-TOF, Chromatography, ELISA, 2DG PAGE, and bioinformatics tools. Challenges are the complexity of the immune system, protein abundance and dynamics, sample variability, post-translational modifications (PTMs), and data integration. Current advancements are enhanced mass spectrometry techniques, single-cell proteomics, artificial intelligence and machine learning, advanced protein labeling techniques, integration with other omics technologies, and functional proteomics. However, the recently emerging field of immunoproteomics has more promising possibilities in the field of peptide-based vaccines and virus-like particle vaccines. The importance of immunoproteomics technologies and methodologies, as well as their use in the field of vaccinomics, are the main topics of this review. Here, we have discussed immunoproteomics in relation to a step towards the future of vaccination.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":"773-795"},"PeriodicalIF":1.0,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142547007","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}