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Facile and versatile ligand analysis method of colloidal quantum dot

Title
Facile and versatile ligand analysis method of colloidal quantum dot
Author(s)
Kim, Jin HaePark, HyokeunKim, Tae-GonLee, HyunmiJun, ShinaeLee, EunhaJeon, Woo SungChung, JaegwanJung, In-Sun
Issued Date
2021-10
Citation
Scientific Reports, v.11, no.1
Type
Article
Keywords
SURFACE-CHEMISTRYQUANTITATIVE-ANALYSISNANOCRYSTALSEXCHANGENMR
ISSN
2045-2322
Abstract
Colloidal quantum-dots (QDs) are highly attractive materials for various optoelectronic applications owing to their easy maneuverability, high functionality, wide applicability, and low cost of mass-production. QDs usually consist of two components: the inorganic nano-crystalline particle and organic ligands that passivate the surface of the inorganic particle. The organic component is also critical for tuning electronic properties of QDs as well as solubilizing QDs in various solvents. However, despite extensive effort to understand the chemistry of ligands, it has been challenging to develop an efficient and reliable method for identifying and quantifying ligands on the QD surface. Herein, we developed a novel method of analyzing ligands in a mild yet accurate fashion. We found that oxidizing agents, as a heterogeneous catalyst in a different phase from QDs, can efficiently disrupt the interaction between the inorganic particle and organic ligands, and the subsequent simple phase fractionation step can isolate the ligand-containing phase from the oxidizer-containing phase and the insoluble precipitates. Our novel analysis procedure ensures to minimize the exposure of ligand molecules to oxidizing agents as well as to prepare homogeneous samples that can be readily analyzed by diverse analytical techniques, such as nuclear magnetic resonance spectroscopy and gas-chromatography mass-spectrometry. © 2021, The Author(s).
URI
http://hdl.handle.net/20.500.11750/15668
DOI
10.1038/s41598-021-99358-x
Publisher
Nature Research
Related Researcher
Files in This Item:
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Appears in Collections:
Department of New Biology Protein Structure Aging Laboratory 1. Journal Articles

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