Pub Date : 2025-11-20DOI: 10.1038/s44286-025-00305-8
iAutoEvoLab is an industrial-grade automation platform for the growth-coupled, continuous evolution of proteins in yeast. Its high throughput, efficiency and effectiveness were demonstrated by the evolution of a DNA-binding protein (LmrA), a lactate sensor (LldR) and a RNA polymerase–capping enzyme fusion protein.
{"title":"iAutoEvoLab as an all-in-one laboratory for programmable protein evolution","authors":"","doi":"10.1038/s44286-025-00305-8","DOIUrl":"10.1038/s44286-025-00305-8","url":null,"abstract":"iAutoEvoLab is an industrial-grade automation platform for the growth-coupled, continuous evolution of proteins in yeast. Its high throughput, efficiency and effectiveness were demonstrated by the evolution of a DNA-binding protein (LmrA), a lactate sensor (LldR) and a RNA polymerase–capping enzyme fusion protein.","PeriodicalId":501699,"journal":{"name":"Nature Chemical Engineering","volume":"2 11","pages":"670-671"},"PeriodicalIF":0.0,"publicationDate":"2025-11-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145561827","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-11-19DOI: 10.1038/s44286-025-00309-4
Yanfei Zhu
{"title":"Layered protection for pure-water electrolysis","authors":"Yanfei Zhu","doi":"10.1038/s44286-025-00309-4","DOIUrl":"10.1038/s44286-025-00309-4","url":null,"abstract":"","PeriodicalId":501699,"journal":{"name":"Nature Chemical Engineering","volume":"2 11","pages":"667-667"},"PeriodicalIF":0.0,"publicationDate":"2025-11-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145561836","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-11-19DOI: 10.1038/s44286-025-00316-5
Mo Qiao
{"title":"Wastewater is a double threat","authors":"Mo Qiao","doi":"10.1038/s44286-025-00316-5","DOIUrl":"10.1038/s44286-025-00316-5","url":null,"abstract":"","PeriodicalId":501699,"journal":{"name":"Nature Chemical Engineering","volume":"2 11","pages":"669-669"},"PeriodicalIF":0.0,"publicationDate":"2025-11-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145561833","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-11-19DOI: 10.1038/s44286-025-00303-w
Da Shen, Xin Wang, Yuan Gao, Wei Wang, Yuchao Li, He Chen, Yushuai Guo, Shuaihua Cao, Yuqing Huang, Yan Zhang, Chengzhi Wang, Shuyi Zhang
Current methods for protein engineering are constrained by limited understanding of sequence–function relationships, the difficulty of designing complex properties by artificial intelligence methods and labor-intensive directed evolution. Here, to enable continuous and scalable protein evolution and systematic exploration of protein adaptive landscapes, we established an industrial-grade automation platform featuring high throughput, high efficiency, enhanced reliability and minimal human intervention (operational for ~1 month). We then developed new genetic circuits for the OrthoRep continuous evolution system to achieve growth-coupled evolution for proteins with diverse and complex functionalities. This included improving lactate sensitivity of LldR via dual selection and increasing operator selectivity for LmrA using the NIMPLY circuit. We integrated these components into an all-in-one laboratory, iAutoEvoLab, and evolved proteins from inactive precursors to fully functional entities, such as a T7 RNA polymerase fusion protein CapT7 with mRNA capping properties, which can be directly applied to in vitro mRNA transcription and mammalian systems. Our system represents a versatile tool for protein engineering and expands the scope for investigating the origins and evolutionary trajectories of protein functions. This study reports on an industrial-grade, large-scale, all-in-one integrated and automated laboratory (iAutoEvoLab), combined with a genetic circuit-controlled, growth-coupled continuous evolution system based on OrthoRep, which can evolve proteins with diverse and complex functionalities. These include protein–protein interactions, protein–DNA interactions, proteins requiring both protein–DNA and protein–ligand interactions, and fusion proteins with low to near-zero activities.
{"title":"An industrial automated laboratory for programmable protein evolution","authors":"Da Shen, Xin Wang, Yuan Gao, Wei Wang, Yuchao Li, He Chen, Yushuai Guo, Shuaihua Cao, Yuqing Huang, Yan Zhang, Chengzhi Wang, Shuyi Zhang","doi":"10.1038/s44286-025-00303-w","DOIUrl":"10.1038/s44286-025-00303-w","url":null,"abstract":"Current methods for protein engineering are constrained by limited understanding of sequence–function relationships, the difficulty of designing complex properties by artificial intelligence methods and labor-intensive directed evolution. Here, to enable continuous and scalable protein evolution and systematic exploration of protein adaptive landscapes, we established an industrial-grade automation platform featuring high throughput, high efficiency, enhanced reliability and minimal human intervention (operational for ~1 month). We then developed new genetic circuits for the OrthoRep continuous evolution system to achieve growth-coupled evolution for proteins with diverse and complex functionalities. This included improving lactate sensitivity of LldR via dual selection and increasing operator selectivity for LmrA using the NIMPLY circuit. We integrated these components into an all-in-one laboratory, iAutoEvoLab, and evolved proteins from inactive precursors to fully functional entities, such as a T7 RNA polymerase fusion protein CapT7 with mRNA capping properties, which can be directly applied to in vitro mRNA transcription and mammalian systems. Our system represents a versatile tool for protein engineering and expands the scope for investigating the origins and evolutionary trajectories of protein functions. This study reports on an industrial-grade, large-scale, all-in-one integrated and automated laboratory (iAutoEvoLab), combined with a genetic circuit-controlled, growth-coupled continuous evolution system based on OrthoRep, which can evolve proteins with diverse and complex functionalities. These include protein–protein interactions, protein–DNA interactions, proteins requiring both protein–DNA and protein–ligand interactions, and fusion proteins with low to near-zero activities.","PeriodicalId":501699,"journal":{"name":"Nature Chemical Engineering","volume":"2 11","pages":"685-698"},"PeriodicalIF":0.0,"publicationDate":"2025-11-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145561837","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-11-19DOI: 10.1038/s44286-025-00323-6
This Editorial showcases recent work on tandem reactor design, highlighting the nuanced role that reactor configuration can play in enabling efficient chemical transformations.
{"title":"One reactor, two reactor","authors":"","doi":"10.1038/s44286-025-00323-6","DOIUrl":"10.1038/s44286-025-00323-6","url":null,"abstract":"This Editorial showcases recent work on tandem reactor design, highlighting the nuanced role that reactor configuration can play in enabling efficient chemical transformations.","PeriodicalId":501699,"journal":{"name":"Nature Chemical Engineering","volume":"2 11","pages":"665-665"},"PeriodicalIF":0.0,"publicationDate":"2025-11-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.nature.comhttps://www.nature.com/articles/s44286-025-00323-6.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145561826","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-11-19DOI: 10.1038/s44286-025-00298-4
Haobo Xu, Rong Yang
Haobo Xu and Rong Yang discuss how scaling laws and chemical engineering fundamentals help control the geometric precision of microdomes by transforming droplets into functional surfaces inspired by nature.
{"title":"Mastering microdomes via scaling laws","authors":"Haobo Xu, Rong Yang","doi":"10.1038/s44286-025-00298-4","DOIUrl":"10.1038/s44286-025-00298-4","url":null,"abstract":"Haobo Xu and Rong Yang discuss how scaling laws and chemical engineering fundamentals help control the geometric precision of microdomes by transforming droplets into functional surfaces inspired by nature.","PeriodicalId":501699,"journal":{"name":"Nature Chemical Engineering","volume":"2 11","pages":"711-711"},"PeriodicalIF":0.0,"publicationDate":"2025-11-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145561828","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-11-19DOI: 10.1038/s44286-025-00310-x
Alessio Lavino
{"title":"Logic gates open to protein biosynthesis","authors":"Alessio Lavino","doi":"10.1038/s44286-025-00310-x","DOIUrl":"10.1038/s44286-025-00310-x","url":null,"abstract":"","PeriodicalId":501699,"journal":{"name":"Nature Chemical Engineering","volume":"2 11","pages":"668-668"},"PeriodicalIF":0.0,"publicationDate":"2025-11-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145561830","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-11-17DOI: 10.1038/s44286-025-00306-7
Gerard Prats Vergel, Huan Mu, Nikita Kolobov, Jasper Biemolt, David A. Vermaas, Thomas Burdyny
Bipolar membranes operated under reverse-bias (r-BPM) provide the only potential route to use anodes free of platinum group metals in CO2 electrolyzers when paired with the oxygen evolution reaction. Under 100% water dissociation efficiency (WDE) conditions, the OH− generated by a r-BPM fully replenishes the OH− consumed by the oxygen evolution reaction, maintaining an alkaline anolyte. However, unwanted co-ion crossover leads to <100% WDEs, gradually causing anolyte acidification and nickel-based anodes to corrode over time. Here we experimentally measured the WDE of r-BPMs in a membrane–electrode assembly configuration as a function of the current density, anolyte concentration and cation identity, finding that the highest measured WDE of 98% is insufficient to maintain an alkaline environment over extended operation. We further highlight through modeling that WDEs >99.8% are required to operate for >10,000 h with reasonable anolyte volumes. Our results show that r-BPMs CO2 electrolyzers require additional strategies, such as reverting to platinum group metal anodes or regenerating the anolyte, to operate stably at an industrial scale. Reverse-biased bipolar membranes can enable CO2 electrolysis with iridium-free anodes for extended durations, but only if 100% of the ionic charge is carried by water dissociation. Here, the authors show that practical systems fall far below unity water dissociation efficiencies, highlighting a performance gap for sustained alkaline operation using nickel-based anodes.
{"title":"Water dissociation efficiencies control the viability of reverse-bias bipolar membranes for CO2 electrolysis","authors":"Gerard Prats Vergel, Huan Mu, Nikita Kolobov, Jasper Biemolt, David A. Vermaas, Thomas Burdyny","doi":"10.1038/s44286-025-00306-7","DOIUrl":"10.1038/s44286-025-00306-7","url":null,"abstract":"Bipolar membranes operated under reverse-bias (r-BPM) provide the only potential route to use anodes free of platinum group metals in CO2 electrolyzers when paired with the oxygen evolution reaction. Under 100% water dissociation efficiency (WDE) conditions, the OH− generated by a r-BPM fully replenishes the OH− consumed by the oxygen evolution reaction, maintaining an alkaline anolyte. However, unwanted co-ion crossover leads to <100% WDEs, gradually causing anolyte acidification and nickel-based anodes to corrode over time. Here we experimentally measured the WDE of r-BPMs in a membrane–electrode assembly configuration as a function of the current density, anolyte concentration and cation identity, finding that the highest measured WDE of 98% is insufficient to maintain an alkaline environment over extended operation. We further highlight through modeling that WDEs >99.8% are required to operate for >10,000 h with reasonable anolyte volumes. Our results show that r-BPMs CO2 electrolyzers require additional strategies, such as reverting to platinum group metal anodes or regenerating the anolyte, to operate stably at an industrial scale. Reverse-biased bipolar membranes can enable CO2 electrolysis with iridium-free anodes for extended durations, but only if 100% of the ionic charge is carried by water dissociation. Here, the authors show that practical systems fall far below unity water dissociation efficiencies, highlighting a performance gap for sustained alkaline operation using nickel-based anodes.","PeriodicalId":501699,"journal":{"name":"Nature Chemical Engineering","volume":"2 11","pages":"676-684"},"PeriodicalIF":0.0,"publicationDate":"2025-11-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.nature.comhttps://www.nature.com/articles/s44286-025-00306-7.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145561831","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-11-04DOI: 10.1038/s44286-025-00307-6
Phase-separation-generated DNA condensates provide a versatile platform for building synthetic cells that mimic crowded intracellular environments. By integrating phase separation with DNA nanotechnology, we have programmed cytoskeleton growth inside synthetic cells. This growth provides switchable and orthogonal architectures that reinforce mechanical stability and can establish robust interfaces with living cells.
{"title":"Using DNA nanotubes to grow cytoskeletons in DNA-based synthetic cells","authors":"","doi":"10.1038/s44286-025-00307-6","DOIUrl":"10.1038/s44286-025-00307-6","url":null,"abstract":"Phase-separation-generated DNA condensates provide a versatile platform for building synthetic cells that mimic crowded intracellular environments. By integrating phase separation with DNA nanotechnology, we have programmed cytoskeleton growth inside synthetic cells. This growth provides switchable and orthogonal architectures that reinforce mechanical stability and can establish robust interfaces with living cells.","PeriodicalId":501699,"journal":{"name":"Nature Chemical Engineering","volume":"2 11","pages":"672-673"},"PeriodicalIF":0.0,"publicationDate":"2025-11-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145561835","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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