SANS partial structure factor analysis for determining protein–polymer interactions in semidilute solution
Name
c9sm00766k.pdf
Description
Published version
Size
3.55 MB
Format
Adobe PDF
Checksum (MD5)
8b08a2c9f0822a6b9c45af66a7680f57
Author(s)
Huang, Aaron
Yao, Helen
Olsen, Bradley D
Date Issued
2019
Journal
Soft Matter
Publisher
Royal Society of Chemistry (RSC)
Version
Final published version
Abstract
© 2019 The Royal Society of Chemistry. The interaction between proteins and polymers in solution contributes to numerous important technological processes, including protein crystallization, biofouling, and the self-assembly of protein-polymer bioconjugates. To quantify these interactions, three different polymers - PNIPAM, POEGA, and PDMAPS - were each blended with a model protein mCherry and studied using contrast variation small angle neutron scattering (SANS). This technique allows for the decomposition of the SANS scattering intensity into partial structure factors corresponding to interactions between two polymer chains, interactions between two proteins, and interactions between a polymer chain and a protein, even for concentrations above the overlap concentration. Examining correlations between each component offers insight into the interactions within the system. In particular, mCherry-PNIPAM interactions are consistent with a depletion interaction, and mCherry-POEGA interactions suggest a considerable region of polymer enrichment close to the protein surface, indicative of attractive forces between the two. Interactions between mCherry and PDMAPS are more complex, with possible contributions from both depletion forces and electrostatic forces.
MIT Department
Massachusetts Institute of Technology. Department of Chemical Engineering
Terms of Use
Creative Commons Attribution 3.0 unported license
Persistent DSpace Link
DOI of Published Version
https://doi.org/10.1039/c9sm00766k
