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Interaction of Globular Plasma Proteins with Water‐Soluble CdSe Quantum Dots
Author(s) -
Pathak Jyotsana,
Rawat Kamla,
Sanwlani Shilpa,
Bohidar H. B.
Publication year - 2015
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.201402629
Subject(s) - chemistry , quantum dot , förster resonance energy transfer , globular protein , molecule , bovine serum albumin , quenching (fluorescence) , fluorescence , tryptophan , dynamic light scattering , crystallography , biophysics , photochemistry , nanoparticle , organic chemistry , amino acid , nanotechnology , chromatography , materials science , biochemistry , physics , quantum mechanics , biology
The interactions between water‐soluble semiconductor quantum dots [hydrophilic 3‐mercaptopropionic acid (MPA)‐coated CdSe] and three globular plasma proteins, namely, bovine serum albumin (BSA), β‐lactoglobulin (β‐Lg) and human serum albumin (HSA), are investigated. Acidic residues of protein molecules form electrostatic interactions with these quantum dots (QDs). To determine the stoichiometry of proteins bound to QDs, we used dynamic light scattering (DLS) and zeta potential techniques. Fluorescence resonance energy transfer (FRET) experiments revealed energy transfer from tryptophan residues in the proteins to the QD particles. Quenching of the intrinsic fluorescence of protein molecules was noticed during this binding process (hierarchy HSA<β‐Lg