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  Investigating the conformation of surface-adsorbed proteins with standing-wave X-ray fluorescence

Scoppola, E., Gochev, G., Drnec, J., Pithan, L., Novikov, D., & Schneck, E. (2021). Investigating the conformation of surface-adsorbed proteins with standing-wave X-ray fluorescence. Biomacromolecules, 22(12), 5195-5203. doi:10.1021/acs.biomac.1c01136.

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 Creators:
Scoppola, Ernesto1, Author              
Gochev, Georgi1, Author              
Drnec, Jakub, Author
Pithan, Linus, Author
Novikov, Dmitri, Author
Schneck, Emanuel1, Author              
Affiliations:
1Emanuel Schneck, Biomaterialien, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_2074300              

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 Abstract: Protein adsorption to surfaces is at the heart of numerous technological and bioanalytical applications, but sometimes, it is also associated with medical risks. To deepen our insights into processes involving layers of surface-adsorbed proteins, high-resolution structural information is essential. Here, we use standing-wave X-ray fluorescence (SWXF) in combination with an optimized liquid-cell setup to investigate the underwater conformation of the random-coiled phosphoprotein β-casein adsorbed to hydrophilic and hydrophobized solid surfaces. The orientation of the protein, as determined through the distributions of sulfur and phosphorus, is found to be sensitive to the chemical nature of the substrate. While no preferred orientations are observed on hydrophobized surfaces, on hydrophilic Al oxide, β-casein is adsorbed as a diblock copolymer with the phosphorylated domain I attached to the surface. Our results demonstrate that targeting biologically relevant chemical elements with SWXF enables a detailed investigation of biomolecular layers under near-physiological conditions.

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Language(s): eng - English
 Dates: 2021-11-232021
 Publication Status: Published in print
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 Identifiers: DOI: 10.1021/acs.biomac.1c01136
BibTex Citekey: doi:10.1021/acs.biomac.1c01136
Other: FDM? Manuskript? angeschrieben 7.12.21 SN
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Title: Biomacromolecules
  Other : Biomacromolecules
Source Genre: Journal
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Publ. Info: Washington, DC : American Chemical Society
Pages: - Volume / Issue: 22 (12) Sequence Number: - Start / End Page: 5195 - 5203 Identifier: ISSN: 1525-7797