Related Experiment Video
Updated: Jun 24, 2026
09:22
Direct Synthesis of EM-Visible Gold Nanoparticles in Cells for Protein Localization Analysis with Well-Preserved Ultrastructure
Published on: April 28, 2023
Interaction of gold nanoparticles with mitochondria
Omer Faruk Karataş1, Erdinç Sezgin, Omer Aydin
1Yeditepe University, Faculty of Engineering and Architecture, Genetics and Bioengineering Department, Kayisdagi, Istanbul, Turkey.
Colloids and Surfaces. B, Biointerfaces
|March 31, 2009
Summary
Surface-enhanced Raman scattering (SERS) can detect gold nanoparticle (GNP) interactions with mitochondria. Although GNPs aggregate in cell cytosol, SERS spectra suggest they may contact mitochondria.
Area of Science:
- Cell Biology
- Nanotechnology
- Biophysics
Background:
- Mitochondria are crucial organelles, and their dysfunction leads to various diseases.
- Understanding nanoparticle interactions with cellular components like mitochondria is vital for nanomedicine.
- Gold nanoparticles (GNPs) are widely studied for biomedical applications.
Purpose of the Study:
- To investigate the feasibility of using surface-enhanced Raman scattering (SERS) to study gold nanoparticle (GNP) interactions with mitochondria.
- To explore the localization and potential contact of GNPs with mitochondria in living cells and isolated mitochondria.
Main Methods:
- Living lung cancer cells and isolated mitochondria were treated with gold colloidal suspension.
- Atomic Force Microscopy (AFM) was used to assess mitochondrial structural integrity.
- Confocal microscopy was employed to determine GNP localization within cells.
- SERS spectroscopy was utilized to analyze molecular changes and interactions.
Main Results:
- AFM confirmed that GNP treatment did not significantly damage mitochondria.
- Confocal microscopy showed GNPs primarily aggregated in the cell cytosol, away from mitochondria.
- SERS spectra from both isolated mitochondria and living cells indicated potential contact between GNPs and mitochondria.
- Evidence suggested GNPs might escape endosomes or enter cells via alternative routes to interact with mitochondria.
Conclusions:
- SERS is a feasible technique for researching mitochondrial functions and interactions.
- Despite cytosolic aggregation, GNPs may interact with mitochondria in living cells.
- Further studies are warranted to elucidate the precise mechanisms of GNP-mitochondria interaction.
Related Concept Videos
01:19Translocation of Proteins into the Mitochondria
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
01:46Electron Transport Chain: Complex I and II
The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
ROS generation is regulated and maintained at moderate levels necessary...
ROS generation is regulated and maintained at moderate levels necessary...
01:28The Inner Mitochondrial Membrane
The inner mitochondrial membrane is the primary site of ATP synthesis. The inner membrane domain that forms a smooth layer adjacent to the outer membrane is called the inner boundary membrane. This domain contains membrane transporters that drive metabolites in and out of the mitochondria. In contrast, the inner membrane network that invaginates into the matrix space is called the cristae membrane. This domain accounts for principle mitochondrial function as it accommodates the protein...
01:45Mitochondrial Membranes
A single mitochondrion is a bean-shaped organelle enclosed by a double-membrane system. The outer membrane of mitochondria is smooth and contains many porins - the integral membrane transporters. Porins enable free diffusion of ions and small uncharged molecules through the outer mitochondrial membrane but limit the transport of molecules larger than 5000 Daltons. Further, the outer mitochondrial membrane forms a unique structure called membrane contact sites with other subcellular organelles,...
01:37Energy to Drive Translocation
Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
Generally, polypeptides are unfolded by two distinct...