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Protein-surfactant-polysaccharide nanoparticles increase the catalytic activity of an engineered β-lactamase maltose-activated switch enzyme

View ORCID ProfileJ.P. Fuenzalida, View ORCID ProfileT. Xiong, View ORCID ProfileB. M. Moerschbacher, View ORCID ProfileMarc Ostermeier, View ORCID ProfileF.M. Goycoolea
doi: https://doi.org/10.1101/746560
J.P. Fuenzalida
*IBBP, Westfälische Wilhelms-Universität Münster Schlossgarten 3, 48149 - Münster, Germany
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T. Xiong
**Department of Chemical & Biomolecular Engineering, Johns Hopkins University, Baltimore, Maryland, USA
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B. M. Moerschbacher
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Marc Ostermeier
**Department of Chemical & Biomolecular Engineering, Johns Hopkins University, Baltimore, Maryland, USA
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  • For correspondence: goycoole@uni-muenster.de oster@jhu.edu
F.M. Goycoolea
*IBBP, Westfälische Wilhelms-Universität Münster Schlossgarten 3, 48149 - Münster, Germany
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  • For correspondence: goycoole@uni-muenster.de oster@jhu.edu
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ABSTRACT

We present polysaccharide-based nanoparticles able to associate and increase the catalytic activity of the maltose-binding MBP317-347 switch enzyme. Fluorescence quenching and molecular docking studies along with the partial resistance to increasing pH and ionic strength indicate that the increase in enzymatic activity is due to a specific interaction between the maltose binding pocket on MBP317-347 and alginate exposed on the surface of the nanoparticles. Finally, we show that the hybrid self co-assembled particles increase the half-life of MBP317-347 over six-fold at 37°C, thus reflecting their potential use as a macromolecular drug delivery system.

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Posted August 24, 2019.
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Protein-surfactant-polysaccharide nanoparticles increase the catalytic activity of an engineered β-lactamase maltose-activated switch enzyme
J.P. Fuenzalida, T. Xiong, B. M. Moerschbacher, Marc Ostermeier, F.M. Goycoolea
bioRxiv 746560; doi: https://doi.org/10.1101/746560
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Protein-surfactant-polysaccharide nanoparticles increase the catalytic activity of an engineered β-lactamase maltose-activated switch enzyme
J.P. Fuenzalida, T. Xiong, B. M. Moerschbacher, Marc Ostermeier, F.M. Goycoolea
bioRxiv 746560; doi: https://doi.org/10.1101/746560

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