Details
| Original language | English |
|---|---|
| Pages (from-to) | 21-35 |
| Number of pages | 15 |
| Journal | RSC Chemical Biology |
| Volume | 6 |
| Issue number | 1 |
| Early online date | 4 Nov 2024 |
| Publication status | Published - 2025 |
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.
ASJC Scopus subject areas
- Chemistry(all)
- Chemistry (miscellaneous)
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry, Genetics and Molecular Biology (miscellaneous)
Sustainable Development Goals
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In: RSC Chemical Biology, Vol. 6, No. 1, 2025, p. 21-35.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - A nanoengineered tandem nitroreductase
T2 - designing a robust prodrug-activating nanoreactor
AU - Zmyslia, Mariia
AU - Capper, Michael J.
AU - Grimmeisen, Michael
AU - Sartory, Kerstin
AU - Deuringer, Benedikt
AU - Abdelsalam, Mohamed
AU - Shen, Kaiwei
AU - Jung, Manfred
AU - Sippl, Wolfgang
AU - Koch, Hans Georg
AU - Kaul, Laurine
AU - Süss, Regine
AU - Köhnke, Jesko
AU - Jessen-Trefzer, Claudia
N1 - Publisher Copyright: © 2024 RSC.
PY - 2025
Y1 - 2025
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85209732654&partnerID=8YFLogxK
U2 - 10.1039/d4cb00127c
DO - 10.1039/d4cb00127c
M3 - Article
AN - SCOPUS:85209732654
VL - 6
SP - 21
EP - 35
JO - RSC Chemical Biology
JF - RSC Chemical Biology
IS - 1
ER -