{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,25]],"date-time":"2026-03-25T02:15:44Z","timestamp":1774404944101,"version":"3.50.1"},"reference-count":52,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2016,4,27]],"date-time":"2016-04-27T00:00:00Z","timestamp":1461715200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Luminescence"],"published-print":{"date-parts":[[2017,2]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>We present here a systematic investigation on the interaction between a water\u2010soluble alloyed semiconductor quantum dot and bovine serum albumin using various spectroscopic techniques i.e. fluorescence quenching, resonance light scattering and synchronous fluorescence spectroscopy. The analysis of fluorescence spectrum and fluorescence intensity indicates that the intrinsic fluorescence of bovine serum albumin (BSA) gets quenched by both static and dynamic quenching mechanism. The Stern\u2010Volmer quenching constants, energy transfer efficiency parameters, binding parameters and corresponding thermodynamic parameters (\u0394<jats:italic>H<\/jats:italic><jats:sup>0<\/jats:sup>, \u0394<jats:italic>S<\/jats:italic><jats:sup>0<\/jats:sup> and \u0394<jats:italic>G<\/jats:italic><jats:sup>0<\/jats:sup>) have been evaluated by using van 't Hoff equation at different temperatures. A positive entropy change with a positive enthalpy change was observed suggesting that the binding process was an entropy\u2010driven, endothermic process associated with the hydrophobic effect. The intermolecular distance (<jats:italic>r<\/jats:italic>) between donor (BSA) and acceptor (CdSeS\/ZnS quantum dots) was estimated according to F\u00f6rster's theory of non\u2010radiative energy transfer. The synchronous fluorescence spectra revealed a blue shift in the emission maxima of tryptophan which is indicative of increasing hydrophobicity. Negative \u0394<jats:italic>G<\/jats:italic><jats:sup>0<\/jats:sup> values implied that the binding process was spontaneous. It was found that hydrophobic forces played a role in the quenching process. Copyright \u00a9 2016 John Wiley &amp; Sons, Ltd.<\/jats:p>","DOI":"10.1002\/bio.3145","type":"journal-article","created":{"date-parts":[[2016,4,27]],"date-time":"2016-04-27T10:41:13Z","timestamp":1461753673000},"page":"35-42","source":"Crossref","is-referenced-by-count":10,"title":["Spectroscopic investigation of water\u2010soluble alloyed QDs with bovine serum albumin"],"prefix":"10.1002","volume":"32","author":[{"given":"K. 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G.","family":"Kotresh","sequence":"additional","affiliation":[{"name":"Laser Spectroscopy Programme &amp; UGC\u2010Centre with Potential for Excellence, Department of Physics Karnatak University  Dharwad 580003 India"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Laxmi S.","family":"Inamdar","sequence":"additional","affiliation":[{"name":"Molecular Endocrinology and Development Laboratory, Department of Zoology Karnatak University  Dharwad 580003 India"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"M. A.","family":"Shivkumar","sequence":"additional","affiliation":[{"name":"Laser Spectroscopy Programme &amp; UGC\u2010Centre with Potential for Excellence, Department of Physics Karnatak University  Dharwad 580003 India"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"B. N.","family":"Jagatap","sequence":"additional","affiliation":[{"name":"Atomic &amp; Molecular Physics Division Bhabha Atomic Research Centre  Mumbai 400 085 India"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"B. G.","family":"Mulimani","sequence":"additional","affiliation":[{"name":"BLDE University  Bijapur India"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"S. 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