{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,14]],"date-time":"2026-10-14T15:10:48Z","timestamp":1791990648316,"version":"4.4.0"},"reference-count":46,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2018,6,21]],"date-time":"2018-06-21T00:00:00Z","timestamp":1529539200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["analyticalsciencejournals.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Luminescence"],"published-print":{"date-parts":[[2018,9]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The binding affinity between bovine serum albumin (BSA) and copper ferrite (CuFe<jats:sub>2<\/jats:sub>O<jats:sub>4<\/jats:sub>) nanoparticles in terms of conformation, stability and activity of protein was studied using various spectroscopic methods. The quenching involved in BSA\u2013CuFe<jats:sub>2<\/jats:sub>O<jats:sub>4<\/jats:sub> NP interaction was static quenching as analysed by different techniques (steady\u2010state and time\u2010resolved fluorescence along with temperature\u2010dependent fluorescence measurements). Among all types of possible interactions, it was revealed that the major binding forces were van der Waals interaction and hydrogen bonding, which were explored from negative values of enthalpy change (\u2206H\u00a0=\u00a0\u2212193.85\u00a0kJ\u00a0mol<jats:sup>\u22121<\/jats:sup>) and entropy change (\u2206S\u00a0=\u00a0\u2212588.88\u00a0J\u00a0mol<jats:sup>\u22121<\/jats:sup>\u00a0K<jats:sup>\u22121<\/jats:sup>). Additionally, synchronous, circular dichroism (CD) and Fourier transform infrared (FTIR) spectroscopy measurements confirmed the conformational changes in BSA upon the addition of CuFe<jats:sub>2<\/jats:sub>O<jats:sub>4<\/jats:sub> NP. Furthermore, thermal denaturation observations were consistent with the circular dichroism results. The interaction of CuFe<jats:sub>2<\/jats:sub>O<jats:sub>4<\/jats:sub> NP with BSA decreased the esterase activity in the BSA assay, revealing the affinity of copper ferrite towards the active site of BSA.<\/jats:p>","DOI":"10.1002\/bio.3499","type":"journal-article","created":{"date-parts":[[2018,6,21]],"date-time":"2018-06-21T10:31:07Z","timestamp":1529577067000},"page":"990-998","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":17,"title":["Insights into the binding interaction between copper ferrite nanoparticles and bovine serum albumin: An effect on protein conformation and activity"],"prefix":"10.1002","volume":"33","author":[{"given":"Sabera","family":"Millan","sequence":"first","affiliation":[{"name":"Department of Chemistry, National Institute of Technology (NIT)  Rourkela Odisha India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aniket","family":"Kumar","sequence":"additional","affiliation":[{"name":"Department of Chemistry, National Institute of Technology (NIT)  Rourkela Odisha India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lakkoji","family":"Satish","sequence":"additional","affiliation":[{"name":"Department of Chemistry, National Institute of Technology (NIT)  Rourkela Odisha India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"B.","family":"Susrisweta","sequence":"additional","affiliation":[{"name":"Department of Chemistry, National Institute of Technology (NIT)  Rourkela Odisha India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Priyabrat","family":"Dash","sequence":"additional","affiliation":[{"name":"Department of Chemistry, National Institute of Technology (NIT)  Rourkela Odisha India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2655-1196","authenticated-orcid":false,"given":"Harekrushna","family":"Sahoo","sequence":"additional","affiliation":[{"name":"Department of Chemistry, National Institute of Technology (NIT)  Rourkela Odisha India"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2018,6,21]]},"reference":[{"key":"e_1_2_7_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbagen.2016.01.027"},{"key":"e_1_2_7_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.ijbiomac.2013.04.064"},{"key":"e_1_2_7_4_1","doi-asserted-by":"publisher","DOI":"10.1186\/1477-3155-11-26"},{"key":"e_1_2_7_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.ijbiomac.2016.11.046"},{"key":"e_1_2_7_6_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.colsurfb.2016.12.030"},{"key":"e_1_2_7_7_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.colsurfb.2014.01.005"},{"key":"e_1_2_7_8_1","doi-asserted-by":"publisher","DOI":"10.1039\/c2cp42415k"},{"key":"e_1_2_7_9_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.actbio.2006.10.006"},{"key":"e_1_2_7_10_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.addr.2008.03.018"},{"key":"e_1_2_7_11_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.apt.2011.04.005"},{"key":"e_1_2_7_12_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmmm.2006.03.036"},{"key":"e_1_2_7_13_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.snb.2007.01.050"},{"key":"e_1_2_7_14_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.colsurfb.2016.02.043"},{"key":"e_1_2_7_15_1","doi-asserted-by":"publisher","DOI":"10.1002\/jat.3299"},{"key":"e_1_2_7_16_1","doi-asserted-by":"publisher","DOI":"10.1007\/s11837-013-0607-2"},{"key":"e_1_2_7_17_1","doi-asserted-by":"publisher","DOI":"10.1021\/bm061084s"},{"key":"e_1_2_7_18_1","doi-asserted-by":"publisher","DOI":"10.1039\/C5RA17254C"},{"key":"e_1_2_7_19_1","first-page":"1","author":"Satish L.","year":"2016","journal-title":"Luminescence"},{"key":"e_1_2_7_20_1","volume-title":"The Plasma Proteins, 2nd ed., (ed. 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