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Related Concept Videos

Translocation of Proteins into the Mitochondria01:19

Translocation 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,...
Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial precursors...
Electron Transport Chain: Complex I and II01:46

Electron 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...
Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death.  Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
Transport of mitochondrial precursors across the TIM23 channel is driven by...
Mitochondrial Membranes01:45

Mitochondrial 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,...

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Related Experiment Video

Updated: May 21, 2026

Experimental Approaches to Study Mitochondrial Localization and Function of a Nuclear Cell Cycle Kinase, Cdk1
13:15

Experimental Approaches to Study Mitochondrial Localization and Function of a Nuclear Cell Cycle Kinase, Cdk1

Published on: February 25, 2016

Mitochondria-Targeting Moieties Based on N-Tethered Pyridinium Cations.

Ivan Džajić1, Natalija Trunkelj1, Jernej Repas1

  • 1Faculty of Pharmacy, University of Ljubljana, Ljubljana, Slovenia.

Angewandte Chemie (International Ed. in English)
|May 20, 2026
PubMed
Summary

New nitrogen cations, like 3,5-diphenylpyridinium (DPPy+), effectively target mitochondria. These DPPy+ moieties show lower intrinsic bioactivity than phosphonium cations, improving mitochondria-targeted therapies and diagnostics.

Keywords:
cancercationsfluorescent probesmedicinal chemistrymitochondria

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Preparation and Evaluation of 99mTc-labeled Tridentate Chelates for Pre-targeting Using Bioorthogonal Chemistry

Published on: February 4, 2017

Area of Science:

  • Mitochondrial biology
  • Chemical biology
  • Drug delivery

Background:

  • Mitochondria-targeting moieties (MTMs) deliver cargo to mitochondria for various applications.
  • Existing MTMs, like phosphonium and nitrogen cations, possess intrinsic bioactivity that can affect cellular functions.
  • Understanding how MTM structure influences distribution and bioactivity is crucial for developing safer and more effective agents.

Purpose of the Study:

  • To systematically evaluate a panel of nitrogen cation-based MTMs.
  • To determine how structural features of N+-based cations affect their subcellular distribution and inherent bioactivity.
  • To identify MTMs with efficient mitochondrial targeting and reduced intrinsic bioactivity for therapeutic applications.

Main Methods:

  • Live-cell imaging of fluorescent dye conjugates to assess cellular uptake and mitochondrial targeting.
  • Profiling of inert cargo derivatives to evaluate effects on mitochondrial membrane potential, oxidative phosphorylation, cellular respiration, and viability.
  • Testing of a Kv1.3 inhibitor conjugate with a novel MTM in cancer cell lines and pancreatic organoid models.

Main Results:

  • 3,5-diphenylpyridinium (DPPy+) demonstrated comparable cellular uptake and mitochondrial targeting to triphenylphosphonium (TPP+).
  • DPPy+ conjugates exhibited lower intrinsic bioactivity on mitochondrial function and cellular respiration compared to TPP+ conjugates.
  • A DPPy+-based Kv1.3 inhibitor conjugate showed enhanced cancer cell apoptosis induction and improved selectivity in pancreatic organoid models.

Conclusions:

  • Lipophilic pyridinium cations, such as DPPy+, serve as effective TPP+ surrogates with improved biocompatibility.
  • DPPy+-based MTMs offer a promising strategy for developing enhanced mitochondria-targeted therapeutic and diagnostic agents.
  • The study highlights structure-dependent lysosomal accumulation of permanent nitrogen cations, informing future MTM design.