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dc.contributor.authorHuang, Aaron
dc.contributor.authorPaloni, Justin Michael
dc.contributor.authorWang, Amy
dc.contributor.authorObermeyer, Allie C
dc.contributor.authorSureka, Hursh Vardhan
dc.contributor.authorYao, Helen
dc.contributor.authorOlsen, Bradley D
dc.date.accessioned2019-09-25T20:30:53Z
dc.date.available2019-09-25T20:30:53Z
dc.date.issued2019-09
dc.date.submitted2019-06
dc.identifier.issn1525-7797
dc.identifier.issn1526-4602
dc.identifier.urihttps://hdl.handle.net/1721.1/122285
dc.description.abstractProtein-polymer bioconjugate self-assembly has attracted a great deal of attention as a method to fabricate protein nanomaterials in solution and the solid state. To identify protein properties that affect phase behavior in protein-polymer block copolymers, a library of 15 unique protein-b-poly(N-isopropylacrylamide) (PNIPAM) copolymers comprising 11 different proteins was compiled and analyzed. Many attributes of phase behavior are found to be similar among all studied bioconjugates regardless of protein properties, such as formation of micellar phases at high temperature and low concentration, lamellar ordering with increasing temperature, and disordering at high concentration, but several key protein-dependent trends are also observed. In particular, hexagonal phases are only observed for proteins within the molar mass range 20-36 kDa, where ordering quality is also significantly enhanced. While ordering is generally found to improve with increasing molecular weight outside of this range, most large bioconjugates exhibited weaker than predicted assembly, which is attributed to chain entanglement with increasing polymer molecular weight. Additionally, order-disorder transition boundaries are found to be largely uncorrelated to protein size and quality of ordering. However, the primary finding is that bioconjugate ordering can be accurately predicted using only protein molecular weight and percentage of residues contained within β sheets. This model provides a basis for designing protein-PNIPAM bioconjugates that exhibit well-defined self-assembly and a modeling framework that can generalize to other bioconjugate chemistries.en_US
dc.description.sponsorshipUnited States. Department of Energy. Office of Basic Energy Sciences (Award DE-SC0007106)en_US
dc.language.isoen
dc.publisherAmerican Chemical Society (ACS)en_US
dc.relation.isversionofhttp://dx.doi.org/10.1021/acs.biomac.9b00768en_US
dc.rightsCreative Commons Attribution-NonCommercial-NoDerivs Licenseen_US
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/en_US
dc.sourceACSen_US
dc.titlePredicting Protein–Polymer Block Copolymer Self-Assembly from Protein Propertiesen_US
dc.typeArticleen_US
dc.identifier.citationHuang, Aaron et al. "Predicting Protein–Polymer Block Copolymer Self-Assembly from Protein Properties." Biomacromolecules (September 2019): 9b000768 © 2019 American Chemical Societyen_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Chemical Engineeringen_US
dc.relation.journalBiomacromoleculesen_US
dc.eprint.versionFinal published versionen_US
dc.type.urihttp://purl.org/eprint/type/JournalArticleen_US
eprint.statushttp://purl.org/eprint/status/PeerRevieweden_US
dc.date.updated2019-09-20T14:14:47Z
dspace.date.submission2019-09-20T14:14:50Z


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