Study of protein adsorption tuned via multivalent ions and the influence of surface charge by XRR and NR

DOI

Protein adsorption at solid-liquid interfaces plays a key role in biomedical technologies such as biosensors or biomaterials for medical implants. Despite considerable progress in this field there are still widely differing and even contradicting opinions on the driving force of protein adsorption at an interface. Protein adsorption to non-biological substrates is even less studied in the presence of multivalent ions. In bulk, globular proteins tuned by multivalent ions how a rich phase behaviour featuring re-entrant condensation and liquid-liquid phase separation (LLPS). This proposal aims to relate the complex bulk phase behaviour to adsorption at an interface and furthermore the interface properties to the adsorption behaviour. Through the joint XRR and NR protein adsorption study, we aim to obtain sufficient contrast variation to fully an analyse our isotope-sensitive system.

Identifier
DOI https://doi.org/10.5286/ISIS.E.95665955
Metadata Access https://icatisis.esc.rl.ac.uk/oaipmh/request?verb=GetRecord&metadataPrefix=oai_datacite&identifier=oai:icatisis.esc.rl.ac.uk:inv/95665955
Provenance
Creator Ms Madeleine Fries; Dr Maxmilian Skoda; Mr Simon Schönberg; Dr Robert Jacobs; Mr Matthias Blum
Publisher ISIS Neutron and Muon Source
Publication Year 2021
Rights CC-BY Attribution 4.0 International; https://creativecommons.org/licenses/by/4.0/
OpenAccess true
Contact isisdata(at)stfc.ac.uk
Representation
Resource Type Dataset
Discipline Biology; Biomaterials; Engineering Sciences; Life Sciences; Materials Science; Materials Science and Engineering; Natural Sciences; Physics
Temporal Coverage Begin 2018-06-06T08:00:00Z
Temporal Coverage End 2018-06-09T08:19:09Z