SANS partial structure factor analysis for determining protein–polymer interactions in semidilute solution
© 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 dif...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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Royal Society of Chemistry (RSC)
2021
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| Online Access: | https://hdl.handle.net/1721.1/136427 |
| _version_ | 1826192874905010176 |
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| author | Huang, Aaron Yao, Helen Olsen, Bradley D |
| author2 | Massachusetts Institute of Technology. Department of Chemical Engineering |
| author_facet | Massachusetts Institute of Technology. Department of Chemical Engineering Huang, Aaron Yao, Helen Olsen, Bradley D |
| author_sort | Huang, Aaron |
| collection | MIT |
| description | © 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. |
| first_indexed | 2024-09-23T09:30:32Z |
| format | Article |
| id | mit-1721.1/136427 |
| institution | Massachusetts Institute of Technology |
| language | English |
| last_indexed | 2024-09-23T09:30:32Z |
| publishDate | 2021 |
| publisher | Royal Society of Chemistry (RSC) |
| record_format | dspace |
| spelling | mit-1721.1/1364272023-02-24T21:32:20Z SANS partial structure factor analysis for determining protein–polymer interactions in semidilute solution Huang, Aaron Yao, Helen Olsen, Bradley D Massachusetts Institute of Technology. Department of Chemical Engineering © 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. 2021-10-27T20:35:19Z 2021-10-27T20:35:19Z 2019 2019-09-10T13:23:07Z Article http://purl.org/eprint/type/JournalArticle https://hdl.handle.net/1721.1/136427 en 10.1039/c9sm00766k Soft Matter Creative Commons Attribution 3.0 unported license https://creativecommons.org/licenses/by/3.0/ application/pdf Royal Society of Chemistry (RSC) Royal Society of Chemistry (RSC) |
| spellingShingle | Huang, Aaron Yao, Helen Olsen, Bradley D SANS partial structure factor analysis for determining protein–polymer interactions in semidilute solution |
| title | SANS partial structure factor analysis for determining protein–polymer interactions in semidilute solution |
| title_full | SANS partial structure factor analysis for determining protein–polymer interactions in semidilute solution |
| title_fullStr | SANS partial structure factor analysis for determining protein–polymer interactions in semidilute solution |
| title_full_unstemmed | SANS partial structure factor analysis for determining protein–polymer interactions in semidilute solution |
| title_short | SANS partial structure factor analysis for determining protein–polymer interactions in semidilute solution |
| title_sort | sans partial structure factor analysis for determining protein polymer interactions in semidilute solution |
| url | https://hdl.handle.net/1721.1/136427 |
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