Nano-Bio Interaction between Blood Plasma Proteins and Water-Soluble Silicon Quantum Dots with Enabled Cellular Uptake and Minimal Cytotoxicity

A better understanding of the compatibility of water-soluble semiconductor quantum dots (QDs) upon contact with the bloodstream is important for biological applications, including biomarkers working in the first therapeutic spectral window for deep tissue imaging. Herein, we investigated the conform...

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Main Authors: Shanmugavel Chinnathambi, Nobutaka Hanagata, Tomohiko Yamazaki, Naoto Shirahata
Format: Article
Language:English
Published: MDPI AG 2020-11-01
Series:Nanomaterials
Subjects:
Online Access:https://www.mdpi.com/2079-4991/10/11/2250
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author Shanmugavel Chinnathambi
Nobutaka Hanagata
Tomohiko Yamazaki
Naoto Shirahata
author_facet Shanmugavel Chinnathambi
Nobutaka Hanagata
Tomohiko Yamazaki
Naoto Shirahata
author_sort Shanmugavel Chinnathambi
collection DOAJ
description A better understanding of the compatibility of water-soluble semiconductor quantum dots (QDs) upon contact with the bloodstream is important for biological applications, including biomarkers working in the first therapeutic spectral window for deep tissue imaging. Herein, we investigated the conformational changes of blood plasma proteins during the interaction with near-infrared light-emitting nanoparticles, consisting of Pluronic F127 shells and cores comprised of assembled silicon QDs terminated with decane monolayers. Albumin and transferrin have high quenching constants and form a hard protein corona on the nanoparticle. In contrast, fibrinogen has low quenching constants and forms a soft protein corona. A circular dichroism (CD) spectrometric study investigates changes in the protein’s secondary and tertiary structures with incremental changes in the nanoparticle concentrations. As expected, the addition of nanoparticles causes the denaturation of the plasma proteins. However, it is noteworthy that the conformational recovery phenomena are observed for fibrinogen and transferrin, suggesting that the nanoparticle does not influence the ordered structure of proteins in the bloodstream. In addition, we observed enabled cellular uptake (NIH3T3 Fibroblasts) and minimal cytotoxicity using different cell lines (HeLa, A549, and NIH3T3). This study offers a basis to design QDs without altering the biomacromolecule’s original conformation with enabled cellular uptake with minimal cytotoxicity.
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spelling doaj.art-69e90107509346bcb437b10ae9a55cae2023-11-20T20:53:28ZengMDPI AGNanomaterials2079-49912020-11-011011225010.3390/nano10112250Nano-Bio Interaction between Blood Plasma Proteins and Water-Soluble Silicon Quantum Dots with Enabled Cellular Uptake and Minimal CytotoxicityShanmugavel Chinnathambi0Nobutaka Hanagata1Tomohiko Yamazaki2Naoto Shirahata3International Center for Young Scientists, National Institute for Materials Science (NIMS), 1-2-1 Sengen, Tsukuba, Ibaraki 305-0047, JapanNanotechnology Innovation Station, NIMS, 1-2-1 Sengen, Tsukuba, Ibaraki 305-0047, JapanGraduate School of Chemical Sciences and Engineering, Hokkaido University, Sapporo 060-0814, JapanGraduate School of Chemical Sciences and Engineering, Hokkaido University, Sapporo 060-0814, JapanA better understanding of the compatibility of water-soluble semiconductor quantum dots (QDs) upon contact with the bloodstream is important for biological applications, including biomarkers working in the first therapeutic spectral window for deep tissue imaging. Herein, we investigated the conformational changes of blood plasma proteins during the interaction with near-infrared light-emitting nanoparticles, consisting of Pluronic F127 shells and cores comprised of assembled silicon QDs terminated with decane monolayers. Albumin and transferrin have high quenching constants and form a hard protein corona on the nanoparticle. In contrast, fibrinogen has low quenching constants and forms a soft protein corona. A circular dichroism (CD) spectrometric study investigates changes in the protein’s secondary and tertiary structures with incremental changes in the nanoparticle concentrations. As expected, the addition of nanoparticles causes the denaturation of the plasma proteins. However, it is noteworthy that the conformational recovery phenomena are observed for fibrinogen and transferrin, suggesting that the nanoparticle does not influence the ordered structure of proteins in the bloodstream. In addition, we observed enabled cellular uptake (NIH3T3 Fibroblasts) and minimal cytotoxicity using different cell lines (HeLa, A549, and NIH3T3). This study offers a basis to design QDs without altering the biomacromolecule’s original conformation with enabled cellular uptake with minimal cytotoxicity.https://www.mdpi.com/2079-4991/10/11/2250siliconquantum dotsplasma proteinsconformational changescell imaging
spellingShingle Shanmugavel Chinnathambi
Nobutaka Hanagata
Tomohiko Yamazaki
Naoto Shirahata
Nano-Bio Interaction between Blood Plasma Proteins and Water-Soluble Silicon Quantum Dots with Enabled Cellular Uptake and Minimal Cytotoxicity
Nanomaterials
silicon
quantum dots
plasma proteins
conformational changes
cell imaging
title Nano-Bio Interaction between Blood Plasma Proteins and Water-Soluble Silicon Quantum Dots with Enabled Cellular Uptake and Minimal Cytotoxicity
title_full Nano-Bio Interaction between Blood Plasma Proteins and Water-Soluble Silicon Quantum Dots with Enabled Cellular Uptake and Minimal Cytotoxicity
title_fullStr Nano-Bio Interaction between Blood Plasma Proteins and Water-Soluble Silicon Quantum Dots with Enabled Cellular Uptake and Minimal Cytotoxicity
title_full_unstemmed Nano-Bio Interaction between Blood Plasma Proteins and Water-Soluble Silicon Quantum Dots with Enabled Cellular Uptake and Minimal Cytotoxicity
title_short Nano-Bio Interaction between Blood Plasma Proteins and Water-Soluble Silicon Quantum Dots with Enabled Cellular Uptake and Minimal Cytotoxicity
title_sort nano bio interaction between blood plasma proteins and water soluble silicon quantum dots with enabled cellular uptake and minimal cytotoxicity
topic silicon
quantum dots
plasma proteins
conformational changes
cell imaging
url https://www.mdpi.com/2079-4991/10/11/2250
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