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Sortase-Mediated Quantifiable Enzyme Immobilization on Magnetic Nanoparticles

Standard

Sortase-Mediated Quantifiable Enzyme Immobilization on Magnetic Nanoparticles. / Fauser, Joel; Savitskiy, Sergey; Fottner, Maximilian; Trauschke, Vanessa; Gulen, Burak.

in: BIOCONJUGATE CHEM, Jahrgang 31, Nr. 8, 19.08.2020, S. 1883-1892.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Fauser, J, Savitskiy, S, Fottner, M, Trauschke, V & Gulen, B 2020, 'Sortase-Mediated Quantifiable Enzyme Immobilization on Magnetic Nanoparticles', BIOCONJUGATE CHEM, Jg. 31, Nr. 8, S. 1883-1892. https://doi.org/10.1021/acs.bioconjchem.0c00322

APA

Fauser, J., Savitskiy, S., Fottner, M., Trauschke, V., & Gulen, B. (2020). Sortase-Mediated Quantifiable Enzyme Immobilization on Magnetic Nanoparticles. BIOCONJUGATE CHEM, 31(8), 1883-1892. https://doi.org/10.1021/acs.bioconjchem.0c00322

Vancouver

Fauser J, Savitskiy S, Fottner M, Trauschke V, Gulen B. Sortase-Mediated Quantifiable Enzyme Immobilization on Magnetic Nanoparticles. BIOCONJUGATE CHEM. 2020 Aug 19;31(8):1883-1892. https://doi.org/10.1021/acs.bioconjchem.0c00322

Bibtex

@article{dc995bf3898c49a691c80a4a347500a5,
title = "Sortase-Mediated Quantifiable Enzyme Immobilization on Magnetic Nanoparticles",
abstract = "Protein immobilization has gained high interest in recent years for its valuable applications in life sciences involving drug delivery and protein arrays. Herein, we combine sortase-mediated protein immobilization with the versatility of magnetic nanoparticles and a sensitive GFP-based quantification system. Using this method, we successfully immobilized and quantified the amount of coupled enzymes by fluorescence spectroscopy and assessed their activity by kinetic measurements. We show that sortase-mediated coupling of enzymes enables preparation of biological samples with a high demand of purity as demonstrated by single-molecule FRET. Here, we report that sortase-mediated protein ligation allows both N- and C-terminal site-specific protein immobilization. Additionally, we demonstrate that sortase-mediated protein immobilization is suitable for direct protein immobilization from complex lysates. Direct immobilization from lysate allows study of enzyme functionality without the need of time-consuming enzyme purification, while magnetic nanoparticles permit easy addition and removal of coupled enzymes to and from a reaction mixture.",
author = "Joel Fauser and Sergey Savitskiy and Maximilian Fottner and Vanessa Trauschke and Burak Gulen",
year = "2020",
month = aug,
day = "19",
doi = "10.1021/acs.bioconjchem.0c00322",
language = "English",
volume = "31",
pages = "1883--1892",
journal = "BIOCONJUGATE CHEM",
issn = "1043-1802",
publisher = "American Chemical Society",
number = "8",

}

RIS

TY - JOUR

T1 - Sortase-Mediated Quantifiable Enzyme Immobilization on Magnetic Nanoparticles

AU - Fauser, Joel

AU - Savitskiy, Sergey

AU - Fottner, Maximilian

AU - Trauschke, Vanessa

AU - Gulen, Burak

PY - 2020/8/19

Y1 - 2020/8/19

N2 - Protein immobilization has gained high interest in recent years for its valuable applications in life sciences involving drug delivery and protein arrays. Herein, we combine sortase-mediated protein immobilization with the versatility of magnetic nanoparticles and a sensitive GFP-based quantification system. Using this method, we successfully immobilized and quantified the amount of coupled enzymes by fluorescence spectroscopy and assessed their activity by kinetic measurements. We show that sortase-mediated coupling of enzymes enables preparation of biological samples with a high demand of purity as demonstrated by single-molecule FRET. Here, we report that sortase-mediated protein ligation allows both N- and C-terminal site-specific protein immobilization. Additionally, we demonstrate that sortase-mediated protein immobilization is suitable for direct protein immobilization from complex lysates. Direct immobilization from lysate allows study of enzyme functionality without the need of time-consuming enzyme purification, while magnetic nanoparticles permit easy addition and removal of coupled enzymes to and from a reaction mixture.

AB - Protein immobilization has gained high interest in recent years for its valuable applications in life sciences involving drug delivery and protein arrays. Herein, we combine sortase-mediated protein immobilization with the versatility of magnetic nanoparticles and a sensitive GFP-based quantification system. Using this method, we successfully immobilized and quantified the amount of coupled enzymes by fluorescence spectroscopy and assessed their activity by kinetic measurements. We show that sortase-mediated coupling of enzymes enables preparation of biological samples with a high demand of purity as demonstrated by single-molecule FRET. Here, we report that sortase-mediated protein ligation allows both N- and C-terminal site-specific protein immobilization. Additionally, we demonstrate that sortase-mediated protein immobilization is suitable for direct protein immobilization from complex lysates. Direct immobilization from lysate allows study of enzyme functionality without the need of time-consuming enzyme purification, while magnetic nanoparticles permit easy addition and removal of coupled enzymes to and from a reaction mixture.

U2 - 10.1021/acs.bioconjchem.0c00322

DO - 10.1021/acs.bioconjchem.0c00322

M3 - SCORING: Journal article

C2 - 32628462

VL - 31

SP - 1883

EP - 1892

JO - BIOCONJUGATE CHEM

JF - BIOCONJUGATE CHEM

SN - 1043-1802

IS - 8

ER -