Impact of polyethylene glycol molecular weight on C-phycocyanin stability

Impact of polyethylene glycol molecular weight on C-phycocyanin stability | Research Square window.SnipcartSettings = { analytics: { enabled: false } }; (function() { var accessVector = localStorage.getItem('access_vector') || ''; window.dataLayer = window.dataLayer || []; if (accessVector) { window.dataLayer.push({ user: { profile: { profileInfo: { snid: accessVector } } } }); } })(); (function(w,d,s,l,i){w[l]=w[l]||[];w[l].push({'gtm.start':new Date().getTime(),event:'gtm.js'});var f=d.getElementsByTagName(s)[0],j=d.createElement(s),dl=l!='dataLayer'?'&l='+l:'';j.async=true;j.src='https://www.googletagmanager.com/gtm.js?id='+i+dl;f.parentNode.insertBefore(j,f);})(window,document,'script','dataLayer','GTM-K279D39R'); Browse Preprints In Review Journals COVID-19 Preprints AJE Video Bytes Research Tools Research Promotion AJE Professional Editing AJE Rubriq About Preprint Platform In Review Editorial Policies Our Team Advisory Board Help Center Sign In Submit a Preprint Cite Share Download PDF Research Article Impact of polyethylene glycol molecular weight on C-phycocyanin stability Mélissa Justin, Adrien Lerbret, Camille Loupiac This is a preprint; it has not been peer reviewed by a journal. https://doi.org/ 10.21203/rs.3.rs-7724448/v1 This work is licensed under a CC BY 4.0 License Status: Under Review Version 1 posted 9 You are reading this latest preprint version Abstract Protein stability depends on both subunit folding and inter-subunit interactions, which are modulated by environmental conditions and cosolutes. This study examined how polyethylene glycols (PEG) of different molecular weights affect the structural stability of the multimeric protein C-phycocyanin (CPC). Using differential scanning calorimetry (DSC), fluorescence spectroscopy, and rheology, we analyzed CPC in the presence of PEG 4 000 g/mol (PEG4) and PEG 35 000 g/mol (PEG35). Fluorescence spectroscopy showed that both PEGs increased the emission intensity of CPC without shifting the emission maximum, indicating changes without major alterations of the global structure. DSC revealed a marked decrease in the enthalpy of unfolding, particularly with PEG35, despite only minor changes in denaturation temperatures. Rheology demonstrated effects of CPC on PEG solution viscosity. The relative increase of the viscosity of PEG4 solution upon addition of CPC is almost two times larger than that of the PEG35. These results suggest that the smaller size and the lower hydration of PEG4 allow it to penetrate more ultimately the hydration shell of CPC, while the larger molecular weight and higher hydration number of PEG35 induce protein–protein association and loss of solubility. Altogether, these results show that PEG molecular weight governs CPC stability: PEG4 may destabilize CPC via crowding and hydration-shell disruption, whereas PEG35 likely reduces CPC solubility through depletion-driven aggregation without altering its folded structure. Full Text Additional Declarations No competing interests reported. Supplementary Files SupplementaryMaterialJustinLerbretLoupiac.docx Cite Share Download PDF Status: Under Review Version 1 posted Editorial decision: Revision requested 22 Oct, 2025 Reviews received at journal 22 Oct, 2025 Reviewers agreed at journal 13 Oct, 2025 Reviews received at journal 13 Oct, 2025 Reviewers agreed at journal 03 Oct, 2025 Reviewers invited by journal 01 Oct, 2025 Editor assigned by journal 29 Sep, 2025 Submission checks completed at journal 29 Sep, 2025 First submitted to journal 26 Sep, 2025 You are reading this latest preprint version Research Square lets you share your work early, gain feedback from the community, and start making changes to your manuscript prior to peer review in a journal. As a division of Research Square Company, we’re committed to making research communication faster, fairer, and more useful. We do this by developing innovative software and high quality services for the global research community. Our growing team is made up of researchers and industry professionals working together to solve the most critical problems facing scientific publishing. Also discoverable on Platform About Our Team In Review Editorial Policies Advisory Board Help Center Resources Author Services Accessibility API Access RSS feed Manage Cookie Preferences © Research Square 2026 | ISSN 2693-5015 (online) Privacy Policy Terms of Service Do Not Sell My Personal Information {"props":{"pageProps":{"initialData":{"identity":"rs-7724448","acceptedTermsAndConditions":true,"allowDirectSubmit":false,"archivedVersions":[],"articleType":"Research Article","associatedPublications":[],"authors":[{"id":529109129,"identity":"e905a147-a376-498a-8710-b0598d61dee5","order_by":0,"name":"Mélissa Justin","email":"","orcid":"","institution":"L’Institut Agro, Univ. 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stability","fulltext":[],"fulltextSource":"","fullText":"","funders":[],"hasAdminPriorityOnWorkflow":false,"hasManuscriptDocX":false,"hasOptedInToPreprint":true,"hasPassedJournalQc":"","hasAnyPriority":false,"hideJournal":false,"highlight":"","institution":"","isAcceptedByJournal":true,"isAuthorSuppliedPdf":true,"isDeskRejected":"","isHiddenFromSearch":false,"isInQc":false,"isInWorkflow":false,"isPdf":true,"isPdfUpToDate":true,"isWithdrawnOrRetracted":false,"journal":{"display":true,"email":"[email protected]","identity":"food-biophysics","isNatureJournal":false,"hasQc":true,"allowDirectSubmit":false,"externalIdentity":"","sideBox":"Learn more about [Food Biophysics](https://www.springer.com/journal/11483)","snPcode":"11483","submissionUrl":"https://submission.nature.com/new-submission/11483/3","title":"Food Biophysics","twitterHandle":"","acdcEnabled":true,"dfaEnabled":true,"editorialSystem":"stoa","reportingPortfolio":"Springer 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This study examined how polyethylene glycols (PEG) of different molecular weights affect the structural stability of the multimeric protein C-phycocyanin (CPC). Using differential scanning calorimetry (DSC), fluorescence spectroscopy, and rheology, we analyzed CPC in the presence of PEG 4 000 g/mol (PEG4) and PEG 35 000 g/mol (PEG35). Fluorescence spectroscopy showed that both PEGs increased the emission intensity of CPC without shifting the emission maximum, indicating changes without major alterations of the global structure. DSC revealed a marked decrease in the enthalpy of unfolding, particularly with PEG35, despite only minor changes in denaturation temperatures. Rheology demonstrated effects of CPC on PEG solution viscosity. The relative increase of the viscosity of PEG4 solution upon addition of CPC is almost two times larger than that of the PEG35. 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