SANS partial structure factor analysis for determining protein–polymer interactions in semidilute solution
Abstract
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.
- Authors:
-
- Department of Chemical Engineering, Massachusetts Institute of Technology, Cambridge, USA
- Publication Date:
- Research Org.:
- Massachusetts Inst. of Technology (MIT), Cambridge, MA (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES)
- OSTI Identifier:
- 1566261
- Alternate Identifier(s):
- OSTI ID: 1801762
- Grant/Contract Number:
- SC0007106
- Resource Type:
- Published Article
- Journal Name:
- Soft Matter
- Additional Journal Information:
- Journal Name: Soft Matter Journal Volume: 15 Journal Issue: 37; Journal ID: ISSN 1744-683X
- Publisher:
- Royal Society of Chemistry (RSC)
- Country of Publication:
- United Kingdom
- Language:
- English
- Subject:
- 37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; 71 CLASSICAL AND QUANTUM MECHANICS, GENERAL PHYSICS; 36 MATERIALS SCIENCE; Chemistry; Materials Science; Physics; Polymer Science
Citation Formats
Huang, Aaron, Yao, Helen, and Olsen, Bradley D. SANS partial structure factor analysis for determining protein–polymer interactions in semidilute solution. United Kingdom: N. p., 2019.
Web. doi:10.1039/C9SM00766K.
Huang, Aaron, Yao, Helen, & Olsen, Bradley D. SANS partial structure factor analysis for determining protein–polymer interactions in semidilute solution. United Kingdom. https://doi.org/10.1039/C9SM00766K
Huang, Aaron, Yao, Helen, and Olsen, Bradley D. Wed .
"SANS partial structure factor analysis for determining protein–polymer interactions in semidilute solution". United Kingdom. https://doi.org/10.1039/C9SM00766K.
@article{osti_1566261,
title = {SANS partial structure factor analysis for determining protein–polymer interactions in semidilute solution},
author = {Huang, Aaron and Yao, Helen and Olsen, Bradley D.},
abstractNote = {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.},
doi = {10.1039/C9SM00766K},
journal = {Soft Matter},
number = 37,
volume = 15,
place = {United Kingdom},
year = {Wed Sep 25 00:00:00 EDT 2019},
month = {Wed Sep 25 00:00:00 EDT 2019}
}
https://doi.org/10.1039/C9SM00766K
Web of Science
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