Inhibition of Albumin Denaturation: Assessing Anti-Inflammatory Activity in collagen for bone regeneration

Inhibition of Albumin Denaturation: Assessing Anti-Inflammatory Activity in collagen for bone regeneration | 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 Inhibition of Albumin Denaturation: Assessing Anti-Inflammatory Activity in collagen for bone regeneration NITHYA M, Dr. ANGELINA GLORITA PARIMALA S This is a preprint; it has not been peer reviewed by a journal. https://doi.org/ 10.21203/rs.3.rs-7751425/v1 This work is licensed under a CC BY 4.0 License Status: Posted Version 1 posted You are reading this latest preprint version Abstract Bone damage often leads to inflammation, which can impede osteogenesis and regeneration. Collagen-based membranes are crucial for guided bone regeneration; However, their efficacy can be compromised by inflammation. This study investigated the anti-inflammatory properties of collagen by assessing its capacity to inhibit heat-induced albumin denaturation, an in vitro model for anti-inflammatory potential, with implications for optimizing the bone healing environment. The anti-inflammatory activity of collagen was evaluated using heat-induced albumin denaturation assay. Various concentrations of thecollagen samples (500, 250, 100, 50, and 10 μg/ml) were tested. Optical density values were measured at 660 nm, and the percentage inhibition of albumin denaturation was calculated. The IC50 values were also determined. The collagen samples demonstrated dose-dependent inhibition of albumin denaturation. As the concentration of collagen decreased, the percentage of inhibition also decreased. This study found an IC50 value of 55.83 μg/ml for the inhibition of albumin denaturation. For example, at 500 μg/ml, the mean inhibition was 55.27%, where as 10 μg/ml, it was 15.23%. Collagen exhibits significant anti-inflammatory properties through its ability to inhibit albumin denaturation, indicating its potential to stabilize proteins and mitigate inflammatory responses crucial for bone regeneration. The IC50 value of 55.83 μg /ml suggests collagen is a potent candidate for therapeutic applications in inflammatory bone conditions, capable of creating an immunomodulatory environment conducive to robust bone remodeling and healing by potentially promoting a pro-regenerative M2 macrophage phenotype. This understanding will inform the design of collagen-based scaffolds that not only provide structural support, but also actively modulate the local inflammatory microenvironment. Anti-inflammatory Albumin denaturation Bone collagen scaffolds Full Text Additional Declarations No competing interests reported. Cite Share Download PDF Status: Posted Version 1 posted 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-7751425","acceptedTermsAndConditions":true,"allowDirectSubmit":true,"archivedVersions":[],"articleType":"Research Article","associatedPublications":[],"authors":[{"id":595466447,"identity":"3f714f30-cd4f-4a1d-9e59-c22e7748d7bf","order_by":0,"name":"NITHYA M","email":"","orcid":"","institution":"A.D.M.COLLEGE FOR WOMEN(AUTONOMOUS)AFFILIATED TO BHARATHIDASAN UNIVERSITY,NAGAPATTINAM,TAMILNADU-611001,INDIA","correspondingAuthor":false,"prefix":"","firstName":"NITHYA","middleName":"","lastName":"M","suffix":""},{"id":595466448,"identity":"760521ac-5044-45d0-bc8f-6c0fbda807cc","order_by":1,"name":"Dr. ANGELINA GLORITA PARIMALA S","email":"data:image/png;base64,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","orcid":"","institution":"A.D.M.COLLEGE FOR WOMEN(AUTONOMOUS)AFFILIATED TO BHARATHIDASAN UNIVERSITY,NAGAPATTINAM,TAMILNADU-611001,INDIA","correspondingAuthor":true,"prefix":"Dr.","firstName":"ANGELINA","middleName":"GLORITA PARIMALA","lastName":"S","suffix":""}],"badges":[],"createdAt":"2025-09-30 12:23:25","currentVersionCode":1,"declarations":"","doi":"10.21203/rs.3.rs-7751425/v1","doiUrl":"https://doi.org/10.21203/rs.3.rs-7751425/v1","draftVersion":[],"editorialEvents":[],"editorialNote":"","failedWorkflow":false,"files":[{"id":105459527,"identity":"ea601134-8c51-4843-9c30-b7d186ae23b5","added_by":"auto","created_at":"2026-03-26 09:43:09","extension":"pdf","order_by":1,"title":"","display":"","copyAsset":false,"role":"manuscript-pdf","size":714612,"visible":true,"origin":"","legend":"","description":"","filename":"NewMicrosoftWordDocument.pdf","url":"https://assets-eu.researchsquare.com/files/rs-7751425/v1_covered_b790d454-9a96-4d6c-83eb-ca10e7abbdee.pdf"}],"financialInterests":"No competing interests reported.","formattedTitle":"Inhibition of Albumin Denaturation: Assessing Anti-Inflammatory Activity in collagen for bone regeneration","fulltext":[],"fulltextSource":"","fullText":"","funders":[],"hasAdminPriorityOnWorkflow":false,"hasManuscriptDocX":false,"hasOptedInToPreprint":true,"hasPassedJournalQc":"","hasAnyPriority":false,"hideJournal":true,"highlight":"","institution":"","isAcceptedByJournal":false,"isAuthorSuppliedPdf":true,"isDeskRejected":"","isHiddenFromSearch":false,"isInQc":false,"isInWorkflow":false,"isPdf":true,"isPdfUpToDate":true,"isWithdrawnOrRetracted":false,"journal":{"display":true,"email":"[email protected]","identity":"researchsquare","isNatureJournal":false,"hasQc":true,"allowDirectSubmit":true,"externalIdentity":"","sideBox":"","snPcode":"","submissionUrl":"/submission","title":"Research Square","twitterHandle":"researchsquare","acdcEnabled":true,"dfaEnabled":false,"editorialSystem":"","reportingPortfolio":"","inReviewEnabled":false,"inReviewRevisionsEnabled":true},"keywords":"Anti-inflammatory, Albumin denaturation, Bone, collagen, scaffolds","lastPublishedDoi":"10.21203/rs.3.rs-7751425/v1","lastPublishedDoiUrl":"https://doi.org/10.21203/rs.3.rs-7751425/v1","license":{"name":"CC BY 4.0","url":"https://creativecommons.org/licenses/by/4.0/"},"manuscriptAbstract":"Bone damage often leads to inflammation, which can impede osteogenesis and regeneration. Collagen-based membranes are crucial for guided bone regeneration; However, their efficacy can be compromised by inflammation. This study investigated the anti-inflammatory properties of collagen by assessing its capacity to inhibit heat-induced albumin denaturation, an in vitro model for anti-inflammatory potential, with implications for optimizing the bone healing environment. The anti-inflammatory activity of collagen was evaluated using heat-induced albumin denaturation assay. Various concentrations of thecollagen samples (500, 250, 100, 50, and 10 μg/ml) were tested. Optical density values were measured at 660 nm, and the percentage inhibition of albumin denaturation was calculated. The IC50 values were also determined. The collagen samples demonstrated dose-dependent inhibition of albumin denaturation. As the concentration of collagen decreased, the percentage of inhibition also decreased. This study found an IC50 value of 55.83 μg/ml for the inhibition of albumin denaturation. For example, at 500 μg/ml, the mean inhibition was 55.27%, where as 10 μg/ml, it was 15.23%. Collagen exhibits significant anti-inflammatory properties through its ability to inhibit albumin denaturation, indicating its potential to stabilize proteins and mitigate inflammatory responses crucial for bone regeneration. The IC50 value of 55.83 μg /ml suggests collagen is a potent candidate for therapeutic applications in inflammatory bone conditions, capable of creating an immunomodulatory environment conducive to robust bone remodeling and healing by potentially promoting a pro-regenerative M2 macrophage phenotype. 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