Interaction of Globular Plasma Proteins with Water-Soluble CdSe Quantum Dots

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 molecu...

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Bibliographic Details
Published in:Chemphyschem 2015-06, Vol.16 (8), p.1777-1786
Main Authors: Pathak, Jyotsana, Rawat, Kamla, Sanwlani, Shilpa, Bohidar, H. B.
Format: Article
Language:English
Subjects:
Binding Sites
Cadmium Compounds - chemistry
conformation analysis
Fluorescence
Humans
hydration
Microscopy, Electron, Transmission
Proteins
Quantum dots
Quantum Dots - chemistry
Quantum Dots - metabolism
secondary structure
Selenium Compounds - chemistry
Serum Albumin - chemistry
Serum Albumin - metabolism
Solubility
Water - chemistry
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Summary: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
ISSN:1439-4235
1439-7641
DOI:10.1002/cphc.201402629