Highly Luminescent Positively Charged Quantum Dots Interacting with Proteins and Cells†. Issue 22 (13th September 2022)
- Record Type:
- Journal Article
- Title:
- Highly Luminescent Positively Charged Quantum Dots Interacting with Proteins and Cells†. Issue 22 (13th September 2022)
- Main Title:
- Highly Luminescent Positively Charged Quantum Dots Interacting with Proteins and Cells†
- Authors:
- Wang, Haixia
Nienhaus, Karin
Shang, Li
Nienhaus, Gerd Ulrich - Abstract:
- Comprehensive Summary: We have studied interactions between positively charged MUTAB‐stabilized quantum dots (QDs) and model proteins, serum and live cells using fluorescence correlation spectroscopy (FCS), dynamic light scattering (DLS), time‐resolved photoluminescence (PL) and live‐cell fluorescence imaging. Using human serum albumin (HSA) as a model protein, we measured the growth of a protein adsorption layer ("protein corona") via time‐resolved FCS. Corona formation was characterized by an apparent equilibrium dissociation coefficient, K D ≈ 10 μM. HSA adlayer growth was surprisingly slow (timescale ca . 30 min), in stark contrast to many similar measurements with HSA and other proteins and different NPs. Time‐resolved PL data revealed a characteristic quenching behavior depending on the QD surface coverage with HSA. Taken together, we found that MUTAB‐QDs initially bind HSA molecules weakly ( K D ≈ 700 μM); however, the affinity is enhanced over time, presumably due to proton injection into the MUTAB layer by HSA triggering ligand dissociation. This process was also observed with human blood serum, showing equal kinetics for comparable HSA concentration. Moreover, imaging experiments with cultured human cells (HeLa) revealed that MUTAB‐QDs bind to the cell membrane and perforate it. This process is reduced upon pre‐adsorption of proteins on the MUTAB‐QD surfaces. Abstract : MUTAB‐capped semiconductor QDs are highly luminescent yet cytotoxic. HSA adsorption decreasesComprehensive Summary: We have studied interactions between positively charged MUTAB‐stabilized quantum dots (QDs) and model proteins, serum and live cells using fluorescence correlation spectroscopy (FCS), dynamic light scattering (DLS), time‐resolved photoluminescence (PL) and live‐cell fluorescence imaging. Using human serum albumin (HSA) as a model protein, we measured the growth of a protein adsorption layer ("protein corona") via time‐resolved FCS. Corona formation was characterized by an apparent equilibrium dissociation coefficient, K D ≈ 10 μM. HSA adlayer growth was surprisingly slow (timescale ca . 30 min), in stark contrast to many similar measurements with HSA and other proteins and different NPs. Time‐resolved PL data revealed a characteristic quenching behavior depending on the QD surface coverage with HSA. Taken together, we found that MUTAB‐QDs initially bind HSA molecules weakly ( K D ≈ 700 μM); however, the affinity is enhanced over time, presumably due to proton injection into the MUTAB layer by HSA triggering ligand dissociation. This process was also observed with human blood serum, showing equal kinetics for comparable HSA concentration. Moreover, imaging experiments with cultured human cells (HeLa) revealed that MUTAB‐QDs bind to the cell membrane and perforate it. This process is reduced upon pre‐adsorption of proteins on the MUTAB‐QD surfaces. Abstract : MUTAB‐capped semiconductor QDs are highly luminescent yet cytotoxic. HSA adsorption decreases both the photoluminescence and the cytotoxicity. … (more)
- Is Part Of:
- Chinese journal of chemistry. Volume 40:Issue 22(2022)
- Journal:
- Chinese journal of chemistry
- Issue:
- Volume 40:Issue 22(2022)
- Issue Display:
- Volume 40, Issue 22 (2022)
- Year:
- 2022
- Volume:
- 40
- Issue:
- 22
- Issue Sort Value:
- 2022-0040-0022-0000
- Page Start:
- 2685
- Page End:
- 2693
- Publication Date:
- 2022-09-13
- Subjects:
- Quantum dots -- Nanoparticles -- Agglomeration -- Protein adsorption -- Quantitative fluorescence microscopy
Chemistry -- Periodicals
540.5 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1614-7065 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/cjoc.202200350 ↗
- Languages:
- English
- ISSNs:
- 1001-604X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3180.299500
British Library DSC - BLDSS-3PM
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