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<article xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:ali="http://www.niso.org/schemas/ali/1.0/" article-type="research-article" dtd-version="1.2" xml:lang="en"><front><journal-meta><journal-id journal-id-type="publisher-id">Current Protein &amp; Peptide Science</journal-id><journal-title-group><journal-title xml:lang="en">Current Protein &amp; Peptide Science</journal-title><trans-title-group xml:lang="ru"><trans-title>Current Protein &amp; Peptide Science</trans-title></trans-title-group></journal-title-group><issn publication-format="print">1389-2037</issn><issn publication-format="electronic">1875-5550</issn><publisher><publisher-name xml:lang="en">Bentham Science</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="publisher-id">645706</article-id><article-id pub-id-type="doi">10.2174/0113892037294778240328041907</article-id><article-categories><subj-group subj-group-type="toc-heading"><subject>Life Sciences</subject></subj-group><subj-group subj-group-type="article-type"><subject>Research Article</subject></subj-group></article-categories><title-group><article-title xml:lang="en">Carboxylic Group Functionalized Carbon Quantum Dots inhibit Hen Egg White Lysozyme Amyloidogenesis, leading to the Formation of Spherical Aggregates with Reduced Toxicity and ROS Generation</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Prabhu</surname><given-names>M.P. Taraka</given-names></name><email>info@benthamscience.net</email><xref ref-type="aff" rid="aff1"/></contrib><contrib contrib-type="author"><name><surname>Chrungoo</surname><given-names>Shreya</given-names></name><email>info@benthamscience.net</email><xref ref-type="aff" rid="aff2"/></contrib><contrib contrib-type="author"><name><surname>Sarkar</surname><given-names>Nandini</given-names></name><email>info@benthamscience.net</email><xref ref-type="aff" rid="aff2"/></contrib></contrib-group><aff id="aff1"><institution>Department of Biotechnology and Medical Engineering,, National Institute of Technology Rourkela</institution></aff><aff id="aff2"><institution>Department of Biotechnology and Medical Engineering, National Institute of Technology Rourkela</institution></aff><pub-date date-type="pub" iso-8601-date="2024-08-01" publication-format="electronic"><day>01</day><month>08</month><year>2024</year></pub-date><volume>25</volume><issue>8</issue><issue-title xml:lang="ru"/><fpage>626</fpage><lpage>637</lpage><history><date date-type="received" iso-8601-date="2025-01-11"><day>11</day><month>01</month><year>2025</year></date></history><permissions><copyright-statement xml:lang="en">Copyright ©; 2024, Bentham Science Publishers</copyright-statement><copyright-year>2024</copyright-year><copyright-holder xml:lang="en">Bentham Science Publishers</copyright-holder><ali:free_to_read xmlns:ali="http://www.niso.org/schemas/ali/1.0/"/></permissions><self-uri xlink:href="https://journals.eco-vector.com/1389-2037/article/view/645706">https://journals.eco-vector.com/1389-2037/article/view/645706</self-uri><abstract xml:lang="en"><p id="idm46466589665728">Introduction::Proteinopathies are a group of diseases where the protein structure has been altered. These alterations are linked to the production of amyloids, which are persistent, organized clumps of protein molecules through inter-molecular interactions. Several disorders, including Alzheimer's and Parkinson's, have been related to the presence of amyloids. Highly ordered beta sheets or beta folds are characteristic of amyloids; these structures can further self- -assemble into stable fibrils.</p><p id="idm46466589669728">Method::Protein aggregation is caused by a wide variety of environmental and experimental factors, including mutations, high pH, high temperature, and chemical modification. Despite several efforts, a cure for amyloidosis has yet to be found. Due to its advantageous semi-conducting characteristics, unique optical features, high surface area-to-volume ratio, biocompatibility, etc., carbon quantum dots (CQDs) have lately emerged as key instruments for a wide range of biomedical applications. To this end, we have investigated the effect of CQDs with a carboxyl group on their surface (CQD-CA) on the in vitro amyloidogenesis of hen egg white lysozyme (HEWL).</p><p id="idm46466589673696">Result::By generating a stable compound that is resistant to fibrillation, our findings show that CQD-CA can suppress amyloid and disaggregate HEWL. In addition, CQD-CA caused the creation of non-toxic spherical aggregates, which generated much less reactive oxygen species (ROS).</p><p id="idm46466589678752">Conclusion::Overall, our results show that more research into amyloidosis treatments, including surface functionalized CQDs, is warranted.</p></abstract><kwd-group xml:lang="en"><kwd>Amyloidogenesis</kwd><kwd>neurodegenerative diseases</kwd><kwd>CQD</kwd><kwd>surface functionalization</kwd><kwd>ROS</kwd><kwd>hen egg white lysozyme</kwd><kwd>proteinopathies.</kwd></kwd-group></article-meta></front><body></body><back><ref-list><ref id="B1"><label>1.</label><mixed-citation>Arosio, P.; Knowles, T.P.J.; Linse, S. On the lag phase in amyloid fibril formation. Phys. Chem. Chem. 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