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Enhanced Luminescent Properties of Photo‐Stable Copper Nanoclusters through Formation of “Protein‐Corona”‐Like Assemblies
Author(s) -
Kumar Das Nirmal,
Chakraborty Subhajit,
Mukherjee Madhumita,
Mukherjee Saptarshi
Publication year - 2018
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.201800332
Subject(s) - dynamic light scattering , nanoclusters , isothermal titration calorimetry , luminescence , chemistry , protein adsorption , human serum albumin , copper , adsorption , nanoparticle , diffusion , fluorescence correlation spectroscopy , titration , chemical physics , analytical chemistry (journal) , molecule , materials science , nanotechnology , organic chemistry , thermodynamics , chromatography , physics , optoelectronics
In this study, interactions of synthesized copper nanoclusters (CuNCs) with a model transport protein, human serum albumin (HSA), have been systematically investigated by using various spectroscopic approaches. The interactions give rise to the formation of “protein‐corona” like assemblies and the luminescence properties (both steady‐state and time‐resolved) are enhanced due to gradual adsorption of the protein on the surface of the NCs. The associated thermodynamics and binding parameters have been estimated resorting to luminescent experimental techniques as well as isothermal titration calorimetry (ITC) studies, indicating that every NC is surrounded by (4±1) protein molecules. The adsorption of HSA on the surface of the NCs has been characterized by dynamic light scattering (DLS) and time‐resolved anisotropy measurements. Finally, fluorescence correlation spectroscopy (FCS) data substantiate the emergence of new “protein‐corona” like assemblies resulting in slower translational diffusion motions and concomitant rise of the hydrodynamic diameters.