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Comprehensively, we studied the interaction between a model protein bovine serum albumin (BSA) and PEGylated toxic free InP\/ZnS QDs using various spectroscopic tools such as absorption, fluorescence quenching, time resolved and synchronous fluorescence spectroscopic measurements. These studies principally show that tryptophan (<jats:italic>Trp<\/jats:italic>) residues of BSA have preferable binding affinity towards PEG\u2010InP\/ZnS QDs surface and a blue shift in <jats:italic>Trp<\/jats:italic> fluorescence emission is a signature of conformational changes in its hydrophobic microenvironment. Photoluminescence (PL) intensity of <jats:italic>Trp<\/jats:italic> is quenched by ground state complex formation (static quenching) at room temperature. However, InP\/ZnS@BSA conjugates become unstable with increasing temperature and PL intensity of <jats:italic>Trp<\/jats:italic> is quenched via dynamic quenching by PEG\u2010InP\/ZnS QDs. Experimentally determined thermodynamic parameters for these conjugates have shown spontaneity, entropy driven and exothermic nature of bio\u2010conjugation. The calculated binding affinity (<jats:italic>n<\/jats:italic> \u2245 1, Hill coefficient) suggest that the affinity of InP\/ZnS QDs for a BSA protein is not dependent on whether or not other BSA proteins are already bound to the QD surface. Energy transfer efficiency (<jats:italic>E<\/jats:italic>), <jats:italic>Trp<\/jats:italic> residue to InP\/ZnS QDs distances and energy transfer rate (<jats:italic>k<\/jats:italic><jats:sub>T<\/jats:sub>) were all obtained from F\u00d6rster resonance energy.<\/jats:p>","DOI":"10.1002\/bio.3438","type":"journal-article","created":{"date-parts":[[2017,12,28]],"date-time":"2017-12-28T03:07:24Z","timestamp":1514430444000},"page":"495-504","source":"Crossref","is-referenced-by-count":13,"title":["Comprehensive study of interaction between biocompatible PEG\u2010InP\/ZnS QDs and bovine serum albumin"],"prefix":"10.1002","volume":"33","author":[{"given":"M. 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