Unknown

Dataset Information

0

Poly(ethylene glycol)-Based Surfactant Reduces the Conformational Change of Adsorbed Proteins on Nanoparticles.


ABSTRACT: When in contact with a biological medium, the surfaces of nanoparticles are usually covered by proteins. In this regard, it was found that poly(ethylene glycol) (PEG) promotes the "stealth effect". This implies a reduction of unspecific protein adsorption and cellular uptake. Although information about the PEG-protein interaction was reported, more accurate and sophisticated structure and dynamics analyses are needed to understand the interaction processes in detail. This work studies the PEG-protein interaction using model nanoparticles stabilized either by the PEG-based surfactant Lutensol AT50 or sodium dodecyl sulfate. The interaction with human serum albumin was studied using neutron scattering techniques. The parameters obtained by small-angle neutron scattering yielded information about the adsorbed protein layer thickness. Protein structure changes were detected via differential scanning fluorimetry and elastic neutron scattering. This combination gives a better insight into the PEG-protein interaction, contributing to the design of nanomaterials for medical applications.

SUBMITTER: Martinez-Negro M 

PROVIDER: S-EPMC9554902 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature

altmetric image

Publications

Poly(ethylene glycol)-Based Surfactant Reduces the Conformational Change of Adsorbed Proteins on Nanoparticles.

Martínez-Negro María M   Russo Daniela D   Prévost Sylvain S   Teixeira José J   Morsbach Svenja S   Landfester Katharina K  

Biomacromolecules 20220909 10


When in contact with a biological medium, the surfaces of nanoparticles are usually covered by proteins. In this regard, it was found that poly(ethylene glycol) (PEG) promotes the "stealth effect". This implies a reduction of unspecific protein adsorption and cellular uptake. Although information about the PEG-protein interaction was reported, more accurate and sophisticated structure and dynamics analyses are needed to understand the interaction processes in detail. This work studies the PEG-pr  ...[more]

Similar Datasets

| S-EPMC3246104 | biostudies-literature
| S-EPMC7678750 | biostudies-literature
| S-EPMC6249031 | biostudies-literature
| S-EPMC6259037 | biostudies-literature
| S-EPMC2276666 | biostudies-literature
| S-EPMC2955982 | biostudies-literature
| S-EPMC7865450 | biostudies-literature
| S-EPMC9657728 | biostudies-literature
| S-EPMC10384068 | biostudies-literature
| S-EPMC7705015 | biostudies-literature