Investigation of trypsin-CdSe quantum dot interactions via spectroscopic methods and effects on enzymatic activity

作者: Gurvir Kaur , S.K. Tripathi

DOI: 10.1016/J.SAA.2014.05.064

关键词: Cadmium selenideBinding constantQuenching (fluorescence)PhotochemistryAcceptorQuantum dotTrypsinFörster resonance energy transferChemistryAnalytical chemistryFluorescence

摘要: The paper presents the interactions between trypsin and water soluble cadmium selenide (CdSe) quantum dots investigated by spectrophotometric methods. CdSe have strong ability to quench intrinsic fluorescence of a static quenching mechanism. has been studied at three different temperatures where results revealed that electrostatic exist are responsible stabilize complex. Scatchard plot from 1 binding site for trypsin, same confirmed making isothermal titrations against trypsin. distance donor acceptor trypsin-CdSe dot complexes is calculated be 2.8 nm energy transfer mechanisms. also enhanced linear concentration ranging 1-80 μl. All observations evidence formation conjugates, retains enzymatic activity which in turn temperature pH dependent.

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