{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,27]],"date-time":"2026-10-27T18:35:01Z","timestamp":1793126101963,"version":"4.5.0"},"reference-count":67,"publisher":"Wiley","issue":"14","license":[{"start":{"date-parts":[[2026,7,26]],"date-time":"2026-07-26T00:00:00Z","timestamp":1785024000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"},{"start":{"date-parts":[[2026,7,26]],"date-time":"2026-07-26T00:00:00Z","timestamp":1785024000000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/501100001412","name":"Council of Scientific and Industrial Research, India","doi-asserted-by":"publisher","award":["01\/2903\/17\/ EMR\u2010II"],"award-info":[{"award-number":["01\/2903\/17\/ EMR\u2010II"]}],"id":[{"id":"10.13039\/501100001412","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["chemistry-europe.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["ChemPhysChem"],"published-print":{"date-parts":[[2026,7,29]]},"abstract":"<jats:p>\n                    Protein misfolding and aggregation are central to many protein aggregation disorders, highlighting the need for effective aggregation inhibitors. This study investigated fructose\u2010induced aggregation of hen egg\u2010white lysozyme (HEWL) and its modulation by the phenolic acids ferulic acid (FA), caffeic acid (CA) and chlorogenic acid (CGA) at 100 and 200\u2009\u03bcM. Circular dichroism and ThT fluorescence assays showed that fructose promoted aggregation through increased \u03b2\u2010sheet content and fluorescence intensity, respectively, whereas all phenolic acids suppressed \u03b2\u2010sheet formation. CA displayed the highest aggregation inhibition activity, followed by FA and CGA. FESEM imaging confirmed fructose\u2010induced HEWL aggregation without fibril formation and demonstrated disruption of aggregates in the presence of phenolic acids. These findings were explained by other biophysical characterisation studies. Fluorescence spectroscopy indicated a static quenching mechanism for all complexes, with FA and CA displaying atypical quenching behaviour. Binding constants suggested moderate affinity, with CA (4.11\u2009\u00b1\u20090.57\u2009\u00d7\u200910\n                    <jats:sup>4<\/jats:sup>\n                    \u2009M\n                    <jats:sup>\u22121<\/jats:sup>\n                    at 300\u2009K) showing the strongest interaction. +\u0394\n                    <jats:italic>S<\/jats:italic>\n                    and +\u0394\n                    <jats:italic>H<\/jats:italic>\n                    indicated hydrophobic interactions as the main stabilising force for all complexes, while computational studies revealed additional H\u2010bonding interactions within aggregation\u2010prone regions (K\u2010peptide) of HEWL. Together, experimental and computational findings demonstrate that these phenolic acids effectively modulate HEWL aggregation by stabilising native\u2010like conformations and disrupting aggregate formation.\n                  <\/jats:p>","DOI":"10.1002\/cphc.70500","type":"journal-article","created":{"date-parts":[[2026,7,26]],"date-time":"2026-07-26T14:51:16Z","timestamp":1785077476000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Complexation of Hen Egg White Lysozyme With Bioactive Phenolic Acids: Molecular Insights Into the Binding Mechanisms and Inhibitory Effects Against Protein Aggregation"],"prefix":"10.1002","volume":"27","author":[{"given":"Sona","family":"Lyndem","sequence":"first","affiliation":[{"name":"Department of Chemical and Biological Sciences National Institute of Technology Meghalaya  Sohra Meghalaya India"},{"name":"Department of Biotechnology St. Anthony's College  Shillong Meghalaya 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