A nanoengineered tandem nitroreductase: designing a robust prodrug-activating nanoreactor

Nitroreductases are important enzymes for a variety of applications, including cancer therapy and bioremediation. They often require encapsulation to improve stability and activity. We focus on genetically encoded encapsulation of nitroreductases within protein capsids, like encapsulins. Our study showcases the encapsulation of nitroreductase NfsB as functional dimers within encapsulins, which enhances protein activity and stability in diverse conditions. Mutations within the pore region are beneficial for activity of the encapsulated enzyme, potentially by increasing diffusion rates. Cryogenic electron microscopy reveals the overall architecture of the encapsulated dimeric NfsB within the nanoreactor environment and identifies multiple pore states in the shell. These findings highlight the potential of encapsulins as versatile tools for enhancing enzyme performance across various fields.

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Publication Details

Journal
RSC Chemical Biology
Published
2024-11-04
DOI
https://doi.org/10.1039/d4cb00127c
Citations
8
Primary Topic
Advanced biosensing and bioanalysis techniques
Type
article
Field-Weighted Citation Impact
1.87

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article

A nanoengineered tandem nitroreductase: designing a robust prodrug-activating nanoreactor

Michael Grimmeisen, Manfred Jung, Mohamed Abdelsalam, Laurine Kaul et al.
8 citations
RSC Chemical Biology
Advanced biosensing and bioanalysis techniques
1.87
article

A nanoengineered tandem nitroreductase: designing a robust prodrug-activating nanoreactor

Michael Grimmeisen, Manfred Jung, Mohamed Abdelsalam, Laurine Kaul, Wolfgang Sippl, Regine Süss, Kaiwei Shen, Hans‐Georg Koch, Claudia Jessen‐Trefzer, Mariia Zmyslia, Michael J. Capper, Benedikt Deuringer, Jesko Köhnke, Kerstin Sartory
article en
8 citations

Abstract

Nitroreductases are important enzymes for a variety of applications, including cancer therapy and bioremediation. They often require encapsulation to improve stability and activity. We focus on genetically encoded encapsulation of nitroreductases within protein capsids, like encapsulins. Our study showcases the encapsulation of nitroreductase NfsB as functional dimers within encapsulins, which enhances protein activity and stability in diverse conditions. Mutations within the pore region are beneficial for activity of the encapsulated enzyme, potentially by increasing diffusion rates. Cryogenic electron microscopy reveals the overall architecture of the encapsulated dimeric NfsB within the nanoreactor environment and identifies multiple pore states in the shell. These findings highlight the potential of encapsulins as versatile tools for enhancing enzyme performance across various fields.

RSC Chemical BiologyVol. 6(1)
Leibniz University Hannover (DE), University of Freiburg (DE), Martin Luther University Halle-Wittenberg (DE), University of Glasgow (GB), Alexandria University (EG)
Ministry of Higher Education and Scientific Research, Scottish Funding Council, Deutscher Akademischer Austauschdienst, Deutsche Forschungsgemeinschaft, Albert-Ludwigs-Universität Freiburg, China Scholarship Council, Medical Research Council, European Research Council
Openalex Percentile: Top 14%
Advanced biosensing and bioanalysis techniques
1.87
DOIOpen Access PDFOpenAlex
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