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Daniel Otzen

Soft Interactions at Nanoparticles Alter Protein Function and Conformation in a Size Dependent Manner

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Soft Interactions at Nanoparticles Alter Protein Function and Conformation in a Size Dependent Manner. / Wang, Jing; Jensen, Uffe B; Jensen, Grethe V; Shipovskov, Stepan; Balakrishnan, Vijay S; Otzen, Daniel; Pedersen, Jan Skov; Besenbacher, Flemming; Sutherland, Duncan S.

In: Nano Letters, Vol. 11, No. 11, 2011, p. 4985-4991.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

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Wang J, Jensen UB, Jensen GV, Shipovskov S, Balakrishnan VS, Otzen D et al. Soft Interactions at Nanoparticles Alter Protein Function and Conformation in a Size Dependent Manner. Nano Letters. 2011;11(11):4985-4991. https://doi.org/10.1021/nl202940k

Author

Wang, Jing ; Jensen, Uffe B ; Jensen, Grethe V ; Shipovskov, Stepan ; Balakrishnan, Vijay S ; Otzen, Daniel ; Pedersen, Jan Skov ; Besenbacher, Flemming ; Sutherland, Duncan S. / Soft Interactions at Nanoparticles Alter Protein Function and Conformation in a Size Dependent Manner. In: Nano Letters. 2011 ; Vol. 11, No. 11. pp. 4985-4991.

Bibtex

@article{4ab2c4352e904deeb45063f8243f6652,
title = "Soft Interactions at Nanoparticles Alter Protein Function and Conformation in a Size Dependent Manner",
abstract = "Weak protein-nanoparticle (NP) interactions are studied in a low binding regime as a model for the soft protein corona around nanoparticles in complex biological fluids. Noncovalent, reversible interactions between Subtilisin Carlsberg (SC) and silica NPs shows significant alteration in conformation and enzymatic activity in a NP-size dependent manner. Very weak interactions between SC and silica NPs were revealed by centrifugation-based separations and further supported by small-angle X-ray scattering, while bovine serum albumin was used as a strongly interacting reference. Secondary and tertiary structure changes of SC were studied via circular dichroism and correlated to enzymatic activity where the enzyme kinetics showed a critical role for nanoparticle size.",
author = "Jing Wang and Jensen, {Uffe B} and Jensen, {Grethe V} and Stepan Shipovskov and Balakrishnan, {Vijay S} and Daniel Otzen and Pedersen, {Jan Skov} and Flemming Besenbacher and Sutherland, {Duncan S}",
year = "2011",
doi = "10.1021/nl202940k",
language = "English",
volume = "11",
pages = "4985--4991",
journal = "Nano Letters",
issn = "1530-6984",
publisher = "AMER CHEMICAL SOC",
number = "11",

}

RIS

TY - JOUR

T1 - Soft Interactions at Nanoparticles Alter Protein Function and Conformation in a Size Dependent Manner

AU - Wang, Jing

AU - Jensen, Uffe B

AU - Jensen, Grethe V

AU - Shipovskov, Stepan

AU - Balakrishnan, Vijay S

AU - Otzen, Daniel

AU - Pedersen, Jan Skov

AU - Besenbacher, Flemming

AU - Sutherland, Duncan S

PY - 2011

Y1 - 2011

N2 - Weak protein-nanoparticle (NP) interactions are studied in a low binding regime as a model for the soft protein corona around nanoparticles in complex biological fluids. Noncovalent, reversible interactions between Subtilisin Carlsberg (SC) and silica NPs shows significant alteration in conformation and enzymatic activity in a NP-size dependent manner. Very weak interactions between SC and silica NPs were revealed by centrifugation-based separations and further supported by small-angle X-ray scattering, while bovine serum albumin was used as a strongly interacting reference. Secondary and tertiary structure changes of SC were studied via circular dichroism and correlated to enzymatic activity where the enzyme kinetics showed a critical role for nanoparticle size.

AB - Weak protein-nanoparticle (NP) interactions are studied in a low binding regime as a model for the soft protein corona around nanoparticles in complex biological fluids. Noncovalent, reversible interactions between Subtilisin Carlsberg (SC) and silica NPs shows significant alteration in conformation and enzymatic activity in a NP-size dependent manner. Very weak interactions between SC and silica NPs were revealed by centrifugation-based separations and further supported by small-angle X-ray scattering, while bovine serum albumin was used as a strongly interacting reference. Secondary and tertiary structure changes of SC were studied via circular dichroism and correlated to enzymatic activity where the enzyme kinetics showed a critical role for nanoparticle size.

U2 - 10.1021/nl202940k

DO - 10.1021/nl202940k

M3 - Journal article

C2 - 21981115

VL - 11

SP - 4985

EP - 4991

JO - Nano Letters

JF - Nano Letters

SN - 1530-6984

IS - 11

ER -