{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,20]],"date-time":"2026-09-20T04:46:51Z","timestamp":1789879611421,"version":"4.0.1"},"reference-count":39,"publisher":"Wiley","issue":"11","license":[{"start":{"date-parts":[[2025,11,7]],"date-time":"2025-11-07T00:00:00Z","timestamp":1762473600000},"content-version":"vor","delay-in-days":6,"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":[[2025,11]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    The binding behavior of the antioxidant supplement chromium picolinate (CPN) with bovine serum albumin (BSA) was examined under simulated physiological conditions using a variety of spectroscopic techniques, including Fourier transform infrared (FTIR), fluorescence, and UV\u2013visible absorption spectroscopy, complemented by molecular docking analyses. Fluorescence quenching studies revealed that the formation of the BSA\u2013CPN complex resulted in the quenching of HSA's intrinsic fluorescence. A portion of the quenching arises from the inner filter effect (IFE), while the remainder occurs through a dynamic mechanism, with a binding affinity of 3.47\u2009\u00d7\u200910\n                    <jats:sup>7<\/jats:sup>\n                    \u2009L\u2009mol\n                    <jats:sup>\u22121<\/jats:sup>\n                    at 298\u2009K. Thermodynamic analysis via the van't Hoff equation provided key parameters, with an enthalpy change (\u0394H\u00b0) of \u2212238.89\u2009kJ\u2009mol\n                    <jats:sup>\u22121<\/jats:sup>\n                    and an entropy change (\u0394S\u00b0) of \u2212671.146\u2009J\u2009mol\n                    <jats:sup>\u22121<\/jats:sup>\n                    \u2009K\n                    <jats:sup>\u22121<\/jats:sup>\n                    . These values, along with spectral data, suggested that the stability of the BSA\u2013CPN complex was primarily governed by hydrogen bonding and van der Waals forces. Further structural analysis using FTIR and UV\u2013vis spectroscopy pointed out that CPN binding made conformational changes in BSA, particularly altering its secondary structure due to interactions with hydrophobic pocket residues. Competitive binding assays with site\u2010specific probes suggested that CPN is likely binding to BSA at a location analogous to Site I.\n                  <\/jats:p>","DOI":"10.1002\/bio.70346","type":"journal-article","created":{"date-parts":[[2025,11,7]],"date-time":"2025-11-07T15:30:13Z","timestamp":1762529413000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Probing the Drug\u2013Protein Interactions Using Multi\u2010Spectroscopic Approaches: Characterizing the Interactions of Chromium Picolinate With Bovine Serum Albumin"],"prefix":"10.1002","volume":"40","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-4741-7298","authenticated-orcid":false,"given":"Nora\u00a0A.","family":"Abdallah","sequence":"first","affiliation":[{"name":"Department of Pharmaceutical Analytical Chemistry, Faculty of Pharmacy Mansoura University  Mansoura Egypt"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3953-7169","authenticated-orcid":false,"given":"Heba","family":"Elmansi","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Analytical Chemistry, Faculty of Pharmacy Mansoura University  Mansoura Egypt"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shahenda\u00a0M.","family":"El\u2010Messery","sequence":"additional","affiliation":[{"name":"Pharmaceutical Organic Chemistry Department, Faculty of Pharmacy Mansoura University  Mansoura Egypt"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fathalla","family":"Belal","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Analytical Chemistry, Faculty of Pharmacy Mansoura University  Mansoura Egypt"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2025,11,7]]},"reference":[{"key":"e_1_2_8_2_1","doi-asserted-by":"publisher","DOI":"10.1201\/b14669"},{"key":"e_1_2_8_3_1","volume-title":"Dietary Reference Intakes for Vitamin A, Vitamin K, Arsenic, Boron, Chromium, Copper, Iodine, Iron, Manganese, Molybdenum, Nickel, Silicon, Vanadium, and Zinc","author":"Standing Committee on the Scientific Evaluation of Dietary Reference Intakes, Subcommittee of Interpretation, Uses of Dietary Reference Intakes, Subcommittee on Upper Reference Levels of Nutrients, & Panel on Micronutrients","year":"2002"},{"key":"e_1_2_8_4_1","doi-asserted-by":"publisher","DOI":"10.1093\/advances\/nmx021"},{"key":"e_1_2_8_5_1","volume-title":"Modern Nutrition in Health and Disease","author":"Ross A. 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