{"title":"不同信号肽在提高重组蛋白在大肠杆菌中溶解度方面的研究:微型综述文章","authors":"Seyyed Soheil Rahmatabadi, Soudabeh Askari, Fatemeh Khademi, Bijan Soleymani","doi":"10.2174/0115701646305738240730113619","DOIUrl":null,"url":null,"abstract":"In E. coli, the production of proteins as inclusion bodies (IBs) caused a decrease in the solubility and activity of these products. Diverse approaches and methods have been used by investigators to overcome this problem. The secretion of recombinant proteins into the periplasmic space by means of suitable signal peptides is a way to resolve these limitations for the production of recombinant proteins in a native form. Secretory production of recombinant proteins in bacterial hosts has many advantages and thus, it is a topic of interest. However, it is hard to achieve due to the difficulty of the process and the need for the choice of appropriate signal peptide for each host and protein. Based on the literature, different signal peptides have experimentally been applied to enhance the solubility of various recombinant proteins. It has been shown that the secretion efficiency of a given protein differs dramatically based on the type of the signal peptide that is attached to the protein. Therefore, the choice and alteration of signal peptides are the two crucial approaches for the improvement of a recombinant protein secretion that have been discussed in this review. Also, different factors affecting the expression and solubility of recombinant proteins have been discussed.","PeriodicalId":50601,"journal":{"name":"Current Proteomics","volume":"57 1","pages":""},"PeriodicalIF":0.5000,"publicationDate":"2024-08-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"The Study of Different Signal Peptides in Improvement of Recombinant Proteins Solubility in E. coli: A Mini-Review Article\",\"authors\":\"Seyyed Soheil Rahmatabadi, Soudabeh Askari, Fatemeh Khademi, Bijan Soleymani\",\"doi\":\"10.2174/0115701646305738240730113619\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"In E. coli, the production of proteins as inclusion bodies (IBs) caused a decrease in the solubility and activity of these products. Diverse approaches and methods have been used by investigators to overcome this problem. The secretion of recombinant proteins into the periplasmic space by means of suitable signal peptides is a way to resolve these limitations for the production of recombinant proteins in a native form. Secretory production of recombinant proteins in bacterial hosts has many advantages and thus, it is a topic of interest. However, it is hard to achieve due to the difficulty of the process and the need for the choice of appropriate signal peptide for each host and protein. Based on the literature, different signal peptides have experimentally been applied to enhance the solubility of various recombinant proteins. It has been shown that the secretion efficiency of a given protein differs dramatically based on the type of the signal peptide that is attached to the protein. Therefore, the choice and alteration of signal peptides are the two crucial approaches for the improvement of a recombinant protein secretion that have been discussed in this review. Also, different factors affecting the expression and solubility of recombinant proteins have been discussed.\",\"PeriodicalId\":50601,\"journal\":{\"name\":\"Current Proteomics\",\"volume\":\"57 1\",\"pages\":\"\"},\"PeriodicalIF\":0.5000,\"publicationDate\":\"2024-08-07\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Current Proteomics\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.2174/0115701646305738240730113619\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"BIOCHEMICAL RESEARCH METHODS\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Current Proteomics","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.2174/0115701646305738240730113619","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOCHEMICAL RESEARCH METHODS","Score":null,"Total":0}
The Study of Different Signal Peptides in Improvement of Recombinant Proteins Solubility in E. coli: A Mini-Review Article
In E. coli, the production of proteins as inclusion bodies (IBs) caused a decrease in the solubility and activity of these products. Diverse approaches and methods have been used by investigators to overcome this problem. The secretion of recombinant proteins into the periplasmic space by means of suitable signal peptides is a way to resolve these limitations for the production of recombinant proteins in a native form. Secretory production of recombinant proteins in bacterial hosts has many advantages and thus, it is a topic of interest. However, it is hard to achieve due to the difficulty of the process and the need for the choice of appropriate signal peptide for each host and protein. Based on the literature, different signal peptides have experimentally been applied to enhance the solubility of various recombinant proteins. It has been shown that the secretion efficiency of a given protein differs dramatically based on the type of the signal peptide that is attached to the protein. Therefore, the choice and alteration of signal peptides are the two crucial approaches for the improvement of a recombinant protein secretion that have been discussed in this review. Also, different factors affecting the expression and solubility of recombinant proteins have been discussed.
Current ProteomicsBIOCHEMICAL RESEARCH METHODS-BIOCHEMISTRY & MOLECULAR BIOLOGY
CiteScore
1.60
自引率
0.00%
发文量
25
审稿时长
>0 weeks
期刊介绍:
Research in the emerging field of proteomics is growing at an extremely rapid rate. The principal aim of Current Proteomics is to publish well-timed in-depth/mini review articles in this fast-expanding area on topics relevant and significant to the development of proteomics. Current Proteomics is an essential journal for everyone involved in proteomics and related fields in both academia and industry.
Current Proteomics publishes in-depth/mini review articles in all aspects of the fast-expanding field of proteomics. All areas of proteomics are covered together with the methodology, software, databases, technological advances and applications of proteomics, including functional proteomics. Diverse technologies covered include but are not limited to:
Protein separation and characterization techniques
2-D gel electrophoresis and image analysis
Techniques for protein expression profiling including mass spectrometry-based methods and algorithms for correlative database searching
Determination of co-translational and post- translational modification of proteins
Protein/peptide microarrays
Biomolecular interaction analysis
Analysis of protein complexes
Yeast two-hybrid projects
Protein-protein interaction (protein interactome) pathways and cell signaling networks
Systems biology
Proteome informatics (bioinformatics)
Knowledge integration and management tools
High-throughput protein structural studies (using mass spectrometry, nuclear magnetic resonance and X-ray crystallography)
High-throughput computational methods for protein 3-D structure as well as function determination
Robotics, nanotechnology, and microfluidics.