Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review
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 newspaper › Journal article › Research › peer-review
}
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 -