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Enzyme-Compatible Dynamic Nanoreactors from Electrostatically Bridged Like-Charged Surfactants and Polyelectrolytes.

Angewandte Chemie (International ed. in English)

Thiele MJ, Davari MD, Hofmann I, König M, Lopez CG, Vojcic L, Richtering W, Schwaneberg U, Tsarkova LA.
PMID: 29889346
Angew Chem Int Ed Engl. 2018 Jul 20;57(30):9402-9407. doi: 10.1002/anie.201805021. Epub 2018 Jul 02.

Reported is an unanticipated mechanism of attractive electrostatic interactions of fully neutralized polyacrylic acid (PAA) with like-charged surfactants. Amphiphilic polymer-surfactant complexes with high interfacial activity and a solubilization capacity exceeding that of conventional micelles are formed by bridging with...

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Thiele MJ, Davari MD, Hofmann I, et al. Enzyme-Compatible Dynamic Nanoreactors from Electrostatically Bridged Like-Charged Surfactants and Polyelectrolytes. Angew Chem Int Ed Engl. 2018;57(30):9402-9407doi: 10.1002/anie.201805021.
Thiele, M. J., Davari, M. D., Hofmann, I., König, M., Lopez, C. G., Vojcic, L., Richtering, W., Schwaneberg, U., & Tsarkova, L. A. (2018). Enzyme-Compatible Dynamic Nanoreactors from Electrostatically Bridged Like-Charged Surfactants and Polyelectrolytes. Angewandte Chemie (International ed. in English), 57(30), 9402-9407. https://doi.org/10.1002/anie.201805021
Thiele, Martin J, et al. "Enzyme-Compatible Dynamic Nanoreactors from Electrostatically Bridged Like-Charged Surfactants and Polyelectrolytes." Angewandte Chemie (International ed. in English) vol. 57,30 (2018): 9402-9407. doi: https://doi.org/10.1002/anie.201805021
Thiele MJ, Davari MD, Hofmann I, König M, Lopez CG, Vojcic L, Richtering W, Schwaneberg U, Tsarkova LA. Enzyme-Compatible Dynamic Nanoreactors from Electrostatically Bridged Like-Charged Surfactants and Polyelectrolytes. Angew Chem Int Ed Engl. 2018 Jul 20;57(30):9402-9407. doi: 10.1002/anie.201805021. Epub 2018 Jul 02. PMID: 29889346.
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KnowVolution Campaign of an Aryl Sulfotransferase Increases Activity toward Cellobiose.

Chemistry (Weinheim an der Bergstrasse, Germany)

Islam S, Laaf D, Infanzón B, Pelantová H, Davari MD, Jakob F, Křen V, Elling L, Schwaneberg U.
PMID: 30153352
Chemistry. 2018 Nov 16;24(64):17117-17124. doi: 10.1002/chem.201803729. Epub 2018 Oct 24.

Sulfated polysaccharides such as cellulose can mimic the functionalities of pathophysiologically important glycosaminoglycans. Enzymatic sulfation offers a green chemistry route to selective (mono)sulfation of oligosaccharides (e.g., cellobiose as a building block of cellulose) in aqueous solution, at ambient temperature,...

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Islam S, Laaf D, Infanzón B, et al. KnowVolution Campaign of an Aryl Sulfotransferase Increases Activity toward Cellobiose. Chemistry. 2018;24(64):17117-17124doi: 10.1002/chem.201803729.
Islam, S., Laaf, D., Infanzón, B., Pelantová, H., Davari, M. D., Jakob, F., Křen, V., Elling, L., & Schwaneberg, U. (2018). KnowVolution Campaign of an Aryl Sulfotransferase Increases Activity toward Cellobiose. Chemistry (Weinheim an der Bergstrasse, Germany), 24(64), 17117-17124. https://doi.org/10.1002/chem.201803729
Islam, Shohana, et al. "KnowVolution Campaign of an Aryl Sulfotransferase Increases Activity toward Cellobiose." Chemistry (Weinheim an der Bergstrasse, Germany) vol. 24,64 (2018): 17117-17124. doi: https://doi.org/10.1002/chem.201803729
Islam S, Laaf D, Infanzón B, Pelantová H, Davari MD, Jakob F, Křen V, Elling L, Schwaneberg U. KnowVolution Campaign of an Aryl Sulfotransferase Increases Activity toward Cellobiose. Chemistry. 2018 Nov 16;24(64):17117-17124. doi: 10.1002/chem.201803729. Epub 2018 Oct 24. PMID: 30153352.
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Notch1 signaling promotes neuro-ectodermal differentiation of embryonic stem cells via the Notch target gene Sox9.

Journal of stem cells & regenerative medicine

Martini S, Schwanbeck R, Main H, Lendahl U, Just U.
PMID: 24693106
J Stem Cells Regen Med. 2010 Oct 23;6(2):88. eCollection 2010.

No abstract available.

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Martini S, Schwanbeck R, Main H, et al. Notch1 signaling promotes neuro-ectodermal differentiation of embryonic stem cells via the Notch target gene Sox9. J Stem Cells Regen Med. 2010;6(2):88
Martini, S., Schwanbeck, R., Main, H., Lendahl, U., & Just, U. (2010). Notch1 signaling promotes neuro-ectodermal differentiation of embryonic stem cells via the Notch target gene Sox9. Journal of stem cells & regenerative medicine, 6(2), 88.
Martini, S, et al. "Notch1 signaling promotes neuro-ectodermal differentiation of embryonic stem cells via the Notch target gene Sox9." Journal of stem cells & regenerative medicine vol. 6,2 (2010): 88.
Martini S, Schwanbeck R, Main H, Lendahl U, Just U. Notch1 signaling promotes neuro-ectodermal differentiation of embryonic stem cells via the Notch target gene Sox9. J Stem Cells Regen Med. 2010 Oct 23;6(2):88. eCollection 2010. PMID: 24693106.
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CaLB Catalyzed Conversion of ε-Caprolactone in Aqueous Medium. Part 1: Immobilization of CaLB to Microgels.

Polymers

Engel S, Höck H, Bocola M, Keul H, Schwaneberg U, Möller M.
PMID: 30974648
Polymers (Basel). 2016 Oct 19;8(10). doi: 10.3390/polym8100372.

The enzymatic ring-opening polymerization of lactones is a method of increasing interest for the synthesis of biodegradable and biocompatible polymers. In the past it was shown that immobilization of

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Engel S, Höck H, Bocola M, et al. CaLB Catalyzed Conversion of ε-Caprolactone in Aqueous Medium. Part 1: Immobilization of CaLB to Microgels. Polymers (Basel). 2016;8(10)doi: 10.3390/polym8100372.
Engel, S., Höck, H., Bocola, M., Keul, H., Schwaneberg, U., & Möller, M. (2016). CaLB Catalyzed Conversion of ε-Caprolactone in Aqueous Medium. Part 1: Immobilization of CaLB to Microgels. Polymers, 8(10), . https://doi.org/10.3390/polym8100372
Engel, Stefan, et al. "CaLB Catalyzed Conversion of ε-Caprolactone in Aqueous Medium. Part 1: Immobilization of CaLB to Microgels." Polymers vol. 8,10 (2016). doi: https://doi.org/10.3390/polym8100372
Engel S, Höck H, Bocola M, Keul H, Schwaneberg U, Möller M. CaLB Catalyzed Conversion of ε-Caprolactone in Aqueous Medium. Part 1: Immobilization of CaLB to Microgels. Polymers (Basel). 2016 Oct 19;8(10). doi: 10.3390/polym8100372. PMID: 30974648; PMCID: PMC6432092.
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[No title available]

Frontiers in microbiology

Schwanbeck J, Oehmig I, Groß U, Zautner AE, Bohne W.
PMID: 34367119
Front Microbiol. 2021 Jul 21;12:715220. doi: 10.3389/fmicb.2021.715220. eCollection 2021.

Flagellar motility is important for the pathogenesis of many intestinal pathogens, allowing bacteria to move to their preferred ecological niche.

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Schwanbeck J, Oehmig I, Groß U, et al. . Front Microbiol. 2021;12:715220doi: 10.3389/fmicb.2021.715220.
Schwanbeck, J., Oehmig, I., Groß, U., Zautner, A. E., & Bohne, W. (2021). . Frontiers in microbiology, 12715220. https://doi.org/10.3389/fmicb.2021.715220
Schwanbeck, Julian, et al. "." Frontiers in microbiology vol. 12 (2021): 715220. doi: https://doi.org/10.3389/fmicb.2021.715220
Schwanbeck J, Oehmig I, Groß U, Zautner AE, Bohne W. . Front Microbiol. 2021 Jul 21;12:715220. doi: 10.3389/fmicb.2021.715220. eCollection 2021. PMID: 34367119; PMCID: PMC8333305.
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Understanding substrate binding and the role of gatekeeping residues in PigC access tunnels.

Chemical communications (Cambridge, England)

Brands S, Sikkens JG, Davari MD, Brass HUC, Klein AS, Pietruszka J, Ruff AJ, Schwaneberg U.
PMID: 33595019
Chem Commun (Camb). 2021 Mar 11;57(21):2681-2684. doi: 10.1039/d0cc08226k.

Semi-rational redesign of the substrate binding pocket and access tunnels of prodigiosin ligase PigC enhanced the catalytic efficiency in the synthesis of pyrrolic anti-cancer agents more than 45 times. A molecular understanding was gained on residues V333 and T334...

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Brands S, Sikkens JG, Davari MD, et al. Understanding substrate binding and the role of gatekeeping residues in PigC access tunnels. Chem Commun (Camb). 2021;57(21):2681-2684doi: 10.1039/d0cc08226k.
Brands, S., Sikkens, J. G., Davari, M. D., Brass, H. U. C., Klein, A. S., Pietruszka, J., Ruff, A. J., & Schwaneberg, U. (2021). Understanding substrate binding and the role of gatekeeping residues in PigC access tunnels. Chemical communications (Cambridge, England), 57(21), 2681-2684. https://doi.org/10.1039/d0cc08226k
Brands, Stefanie, et al. "Understanding substrate binding and the role of gatekeeping residues in PigC access tunnels." Chemical communications (Cambridge, England) vol. 57,21 (2021): 2681-2684. doi: https://doi.org/10.1039/d0cc08226k
Brands S, Sikkens JG, Davari MD, Brass HUC, Klein AS, Pietruszka J, Ruff AJ, Schwaneberg U. Understanding substrate binding and the role of gatekeeping residues in PigC access tunnels. Chem Commun (Camb). 2021 Mar 11;57(21):2681-2684. doi: 10.1039/d0cc08226k. PMID: 33595019.
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Detection of a New Resistance-Mediating Plasmid Chimera in a .

Microorganisms

Schwanbeck J, Bohne W, Hasdemir U, Groß U, Pfeifer Y, Bunk B, Riedel T, Spröer C, Overmann J, Frickmann H, Zautner AE.
PMID: 33807212
Microorganisms. 2021 Mar 31;9(4). doi: 10.3390/microorganisms9040720.

Mobile genetic elements, such as plasmids, facilitate the spread of antibiotic resistance genes in Enterobacterales. In line with this, we investigated the plasmid-resistome of seven

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Schwanbeck J, Bohne W, Hasdemir U, et al. Detection of a New Resistance-Mediating Plasmid Chimera in a . Microorganisms. 2021;9(4)doi: 10.3390/microorganisms9040720.
Schwanbeck, J., Bohne, W., Hasdemir, U., Groß, U., Pfeifer, Y., Bunk, B., Riedel, T., Spröer, C., Overmann, J., Frickmann, H., & Zautner, A. E. (2021). Detection of a New Resistance-Mediating Plasmid Chimera in a . Microorganisms, 9(4), . https://doi.org/10.3390/microorganisms9040720
Schwanbeck, Julian, et al. "Detection of a New Resistance-Mediating Plasmid Chimera in a ." Microorganisms vol. 9,4 (2021). doi: https://doi.org/10.3390/microorganisms9040720
Schwanbeck J, Bohne W, Hasdemir U, Groß U, Pfeifer Y, Bunk B, Riedel T, Spröer C, Overmann J, Frickmann H, Zautner AE. Detection of a New Resistance-Mediating Plasmid Chimera in a . Microorganisms. 2021 Mar 31;9(4). doi: 10.3390/microorganisms9040720. PMID: 33807212; PMCID: PMC8066831.
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Unraveling the Mechanism and Kinetics of Binding of an LCI-eGFP-Polymer for Antifouling Coatings.

Macromolecular bioscience

Söder D, Garay-Sarmiento M, Rahimi K, Obstals F, Dedisch S, Haraszti T, Davari MD, Jakob F, Heß C, Schwaneberg U, Rodriguez-Emmenegger C.
PMID: 34145970
Macromol Biosci. 2021 Sep;21(9):e2100158. doi: 10.1002/mabi.202100158. Epub 2021 Jun 18.

The ability of proteins to adsorb irreversibly onto surfaces opens new possibilities to functionalize biological interfaces. Herein, the mechanism and kinetics of adsorption of protein-polymer macromolecules with the ability to equip surfaces with antifouling properties are investigated. These macromolecules...

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Söder D, Garay-Sarmiento M, Rahimi K, et al. Unraveling the Mechanism and Kinetics of Binding of an LCI-eGFP-Polymer for Antifouling Coatings. Macromol Biosci. 2021;21(9):e2100158doi: 10.1002/mabi.202100158.
Söder, D., Garay-Sarmiento, M., Rahimi, K., Obstals, F., Dedisch, S., Haraszti, T., Davari, M. D., Jakob, F., Heß, C., Schwaneberg, U., & Rodriguez-Emmenegger, C. (2021). Unraveling the Mechanism and Kinetics of Binding of an LCI-eGFP-Polymer for Antifouling Coatings. Macromolecular bioscience, 21(9), e2100158. https://doi.org/10.1002/mabi.202100158
Söder, Dominik, et al. "Unraveling the Mechanism and Kinetics of Binding of an LCI-eGFP-Polymer for Antifouling Coatings." Macromolecular bioscience vol. 21,9 (2021): e2100158. doi: https://doi.org/10.1002/mabi.202100158
Söder D, Garay-Sarmiento M, Rahimi K, Obstals F, Dedisch S, Haraszti T, Davari MD, Jakob F, Heß C, Schwaneberg U, Rodriguez-Emmenegger C. Unraveling the Mechanism and Kinetics of Binding of an LCI-eGFP-Polymer for Antifouling Coatings. Macromol Biosci. 2021 Sep;21(9):e2100158. doi: 10.1002/mabi.202100158. Epub 2021 Jun 18. PMID: 34145970.
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Using Molecular Simulation to Guide Protein Engineering for Biocatalysis in Organic Solvents.

Methods in molecular biology (Clifton, N.J.)

Cui H, Vedder M, Schwaneberg U, Davari MD.
PMID: 34813065
Methods Mol Biol. 2022;2397:179-202. doi: 10.1007/978-1-0716-1826-4_10.

Biocatalysis in organic solvents (OSs) is very appealing for the industry in producing bulk and/or fine chemicals, such as pharmaceuticals, biodiesel, and fragrances. The poor performance of enzymes in OSs (e.g., reduced activity, insufficient stability, and deactivation) negates OSs'...

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Cui H, Vedder M, Schwaneberg U, et al. Using Molecular Simulation to Guide Protein Engineering for Biocatalysis in Organic Solvents. Methods Mol Biol. 2022;2397:179-202doi: 10.1007/978-1-0716-1826-4_10.
Cui, H., Vedder, M., Schwaneberg, U., & Davari, M. D. (2022). Using Molecular Simulation to Guide Protein Engineering for Biocatalysis in Organic Solvents. Methods in molecular biology (Clifton, N.J.), 2397179-202. https://doi.org/10.1007/978-1-0716-1826-4_10
Cui, Haiyang, et al. "Using Molecular Simulation to Guide Protein Engineering for Biocatalysis in Organic Solvents." Methods in molecular biology (Clifton, N.J.) vol. 2397 (2022): 179-202. doi: https://doi.org/10.1007/978-1-0716-1826-4_10
Cui H, Vedder M, Schwaneberg U, Davari MD. Using Molecular Simulation to Guide Protein Engineering for Biocatalysis in Organic Solvents. Methods Mol Biol. 2022;2397:179-202. doi: 10.1007/978-1-0716-1826-4_10. PMID: 34813065.
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Phytase blends for enhanced phosphorous mobilization of deoiled seeds.

Enzyme and microbial technology

Infanzón B, Herrmann KR, Hofmann I, Willbold S, Ruff AJ, Schwaneberg U.
PMID: 34847439
Enzyme Microb Technol. 2022 Jan;153:109953. doi: 10.1016/j.enzmictec.2021.109953. Epub 2021 Nov 23.

Phytases are hydrolytic enzymes capable of a stepwise phosphate release from phytate which is the main phosphorous storage in seeds, cereals and legumes. Limitations such as low enzyme activity or incomplete phytate hydrolysis to inositol are a great challenge...

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Infanzón B, Herrmann KR, Hofmann I, et al. Phytase blends for enhanced phosphorous mobilization of deoiled seeds. Enzyme Microb Technol. 2021;153:109953doi: 10.1016/j.enzmictec.2021.109953.
Infanzón, B., Herrmann, K. R., Hofmann, I., Willbold, S., Ruff, A. J., & Schwaneberg, U. (2022). Phytase blends for enhanced phosphorous mobilization of deoiled seeds. Enzyme and microbial technology, 153109953. https://doi.org/10.1016/j.enzmictec.2021.109953
Infanzón, Belén, et al. "Phytase blends for enhanced phosphorous mobilization of deoiled seeds." Enzyme and microbial technology vol. 153 (2022): 109953. doi: https://doi.org/10.1016/j.enzmictec.2021.109953
Infanzón B, Herrmann KR, Hofmann I, Willbold S, Ruff AJ, Schwaneberg U. Phytase blends for enhanced phosphorous mobilization of deoiled seeds. Enzyme Microb Technol. 2022 Jan;153:109953. doi: 10.1016/j.enzmictec.2021.109953. Epub 2021 Nov 23. PMID: 34847439.
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Aqueous ionic liquids redistribute local enzyme stability via long-range perturbation pathways.

Computational and structural biotechnology journal

El Harrar T, Frieg B, Davari MD, Jaeger KE, Schwaneberg U, Gohlke H.
PMID: 34429845
Comput Struct Biotechnol J. 2021 Jul 08;19:4248-4264. doi: 10.1016/j.csbj.2021.07.001. eCollection 2021.

Ionic liquids (IL) and aqueous ionic liquids (aIL) are attractive (co-)solvents for biocatalysis due to their unique properties. On the other hand, the incubation of enzymes in IL or aIL often reduces enzyme activity. Recent studies proposed various aIL-induced...

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El Harrar T, Frieg B, Davari MD, et al. Aqueous ionic liquids redistribute local enzyme stability via long-range perturbation pathways. Comput Struct Biotechnol J. 2021;19:4248-4264doi: 10.1016/j.csbj.2021.07.001.
El Harrar, T., Frieg, B., Davari, M. D., Jaeger, K. E., Schwaneberg, U., & Gohlke, H. (2021). Aqueous ionic liquids redistribute local enzyme stability via long-range perturbation pathways. Computational and structural biotechnology journal, 194248-4264. https://doi.org/10.1016/j.csbj.2021.07.001
El Harrar, Till, et al. "Aqueous ionic liquids redistribute local enzyme stability via long-range perturbation pathways." Computational and structural biotechnology journal vol. 19 (2021): 4248-4264. doi: https://doi.org/10.1016/j.csbj.2021.07.001
El Harrar T, Frieg B, Davari MD, Jaeger KE, Schwaneberg U, Gohlke H. Aqueous ionic liquids redistribute local enzyme stability via long-range perturbation pathways. Comput Struct Biotechnol J. 2021 Jul 08;19:4248-4264. doi: 10.1016/j.csbj.2021.07.001. eCollection 2021. PMID: 34429845; PMCID: PMC8355836.
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Computer-Assisted Recombination (CompassR) Teaches us How to Recombine Beneficial Substitutions from Directed Evolution Campaigns.

Chemistry (Weinheim an der Bergstrasse, Germany)

Cui H, Cao H, Cai H, Jaeger KE, Davari MD, Schwaneberg U.
PMID: 31553080
Chemistry. 2020 Jan 13;26(3):643-649. doi: 10.1002/chem.201903994. Epub 2019 Dec 03.

A main remaining challenge in protein engineering is how to recombine beneficial substitutions. Systematic recombination studies show that poorly performing variants are usually obtained after recombination of 3 to 4 beneficial substitutions. This limits researchers in exploiting nature's potential...

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Cui H, Cao H, Cai H, et al. Computer-Assisted Recombination (CompassR) Teaches us How to Recombine Beneficial Substitutions from Directed Evolution Campaigns. Chemistry. 2019;26(3):643-649doi: 10.1002/chem.201903994.
Cui, H., Cao, H., Cai, H., Jaeger, K. E., Davari, M. D., & Schwaneberg, U. (2020). Computer-Assisted Recombination (CompassR) Teaches us How to Recombine Beneficial Substitutions from Directed Evolution Campaigns. Chemistry (Weinheim an der Bergstrasse, Germany), 26(3), 643-649. https://doi.org/10.1002/chem.201903994
Cui, Haiyang, et al. "Computer-Assisted Recombination (CompassR) Teaches us How to Recombine Beneficial Substitutions from Directed Evolution Campaigns." Chemistry (Weinheim an der Bergstrasse, Germany) vol. 26,3 (2020): 643-649. doi: https://doi.org/10.1002/chem.201903994
Cui H, Cao H, Cai H, Jaeger KE, Davari MD, Schwaneberg U. Computer-Assisted Recombination (CompassR) Teaches us How to Recombine Beneficial Substitutions from Directed Evolution Campaigns. Chemistry. 2020 Jan 13;26(3):643-649. doi: 10.1002/chem.201903994. Epub 2019 Dec 03. PMID: 31553080; PMCID: PMC7003928.
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