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Title: SANS partial structure factor analysis for determining protein–polymer interactions in semidilute solution

Journal Article · · Soft Matter
DOI: https://doi.org/10.1039/c9sm00766k · OSTI ID:1566261

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.

Research Organization:
Massachusetts Inst. of Technology (MIT), Cambridge, MA (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Basic Energy Sciences (BES)
Grant/Contract Number:
SC0007106
OSTI ID:
1566261
Alternate ID(s):
OSTI ID: 1801762
Journal Information:
Soft Matter, Vol. 15, Issue 37; ISSN 1744-683X
Publisher:
Royal Society of ChemistryCopyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 7 works
Citation information provided by
Web of Science

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