Effects of Protein Unfolding on Aggregation and Gelation in Lysozyme Solutions

dc.contributor.authorNikfarjam, Shakiba
dc.contributor.authorJouravleva, Elena V.
dc.contributor.authorAnisimov, Mikhail A.
dc.contributor.authorWoehl, Taylor J.
dc.date.accessioned2023-11-08T19:18:04Z
dc.date.available2023-11-08T19:18:04Z
dc.date.issued2020-09-02
dc.description.abstractIn this work, we investigate the role of folding/unfolding equilibrium in protein aggregation and formation of a gel network. Near the neutral pH and at a low buffer ionic strength, the formation of the gel network around unfolding conditions prevents investigations of protein aggregation. In this study, by deploying the fact that in lysozyme solutions the time of folding/unfolding is much shorter than the characteristic time of gelation, we have prevented gelation by rapidly heating the solution up to the unfolding temperature (~80 °C) for a short time (~30 min.) followed by fast cooling to the room temperature. Dynamic light scattering measurements show that if the gelation is prevented, nanosized irreversible aggregates (about 10–15 nm radius) form over a time scale of 10 days. These small aggregates persist and aggregate further into larger aggregates over several weeks. If gelation is not prevented, the nanosized aggregates become the building blocks for the gel network and define its mesh length scale. These results support our previously published conclusion on the nature of mesoscopic aggregates commonly observed in solutions of lysozyme, namely that aggregates do not form from lysozyme monomers in their native folded state. Only with the emergence of a small fraction of unfolded proteins molecules will the aggregates start to appear and grow.
dc.description.urihttps://doi.org/10.3390/biom10091262
dc.identifierhttps://doi.org/10.13016/dspace/ounh-axyl
dc.identifier.citationNikfarjam, S.; Jouravleva, E.V.; Anisimov, M.A.; Woehl, T.J. Effects of Protein Unfolding on Aggregation and Gelation in Lysozyme Solutions. Biomolecules 2020, 10, 1262.
dc.identifier.urihttp://hdl.handle.net/1903/31318
dc.language.isoen_US
dc.publisherMDPI
dc.relation.isAvailableAtDigital Repository at the University of Marylanden_us
dc.relation.isAvailableAtUniversity of Maryland (College Park, MD)en_us
dc.relation.isAvailableAtA. James Clark School of Engineeringen_us
dc.relation.isAvailableAtChemical & Biomolecular Engineeringen_us
dc.subjectlysozyme
dc.subjectaggregation
dc.subjectgelation
dc.subjectprotein folding/unfolding
dc.titleEffects of Protein Unfolding on Aggregation and Gelation in Lysozyme Solutions
dc.typeArticle
local.equitableAccessSubmissionNo

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