Aleksandra Chorążewska, Darragh Regan, Marta Kalka, Krzysztof Ciura, Natalia Porębska, Łukasz Opaliński
{"title":"Thermostable phenylacetic acid degradation protein TtPaaI from Thermus thermophilus as a scaffold for tetravalent display of proteins","authors":"Aleksandra Chorążewska, Darragh Regan, Marta Kalka, Krzysztof Ciura, Natalia Porębska, Łukasz Opaliński","doi":"10.1016/j.pep.2024.106623","DOIUrl":null,"url":null,"abstract":"<div><div>Numerous proteins in nature strictly require oligomerization for their full activity. Moreover, the function of natural and artificial proteins can me adjusted by altering their oligomeric state, leading to development of biotechnologically-relevant biomacromolecules. Oligomerization scaffolds from natural sources and designed <em>de novo</em> enable shuffling the oligomeric state and valency of biomacromolecules. In this report we probed the scaffolding potential of the thermostable phenylacetic acid degradation protein acyl-CoA from <em>Thermus thermophilus</em> (<em>Tt</em>PaaI). We designed and successfully produced the fusion protein between <em>Tt</em>PaaI (scaffold) and galectin-7, a multifunctional lectin implicated in human diseases (ligand) and demonstrated that <em>Tt</em>PaaI can serve as a framework for functional multivalent display of ligands.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"227 ","pages":"Article 106623"},"PeriodicalIF":1.4000,"publicationDate":"2024-11-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Protein expression and purification","FirstCategoryId":"99","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S1046592824001955","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}
引用次数: 0
Abstract
Numerous proteins in nature strictly require oligomerization for their full activity. Moreover, the function of natural and artificial proteins can me adjusted by altering their oligomeric state, leading to development of biotechnologically-relevant biomacromolecules. Oligomerization scaffolds from natural sources and designed de novo enable shuffling the oligomeric state and valency of biomacromolecules. In this report we probed the scaffolding potential of the thermostable phenylacetic acid degradation protein acyl-CoA from Thermus thermophilus (TtPaaI). We designed and successfully produced the fusion protein between TtPaaI (scaffold) and galectin-7, a multifunctional lectin implicated in human diseases (ligand) and demonstrated that TtPaaI can serve as a framework for functional multivalent display of ligands.
期刊介绍:
Protein Expression and Purification is an international journal providing a forum for the dissemination of new information on protein expression, extraction, purification, characterization, and/or applications using conventional biochemical and/or modern molecular biological approaches and methods, which are of broad interest to the field. The journal does not typically publish repetitive examples of protein expression and purification involving standard, well-established, methods. However, exceptions might include studies on important and/or difficult to express and/or purify proteins and/or studies that include extensive protein characterization, which provide new, previously unpublished information.