Related Experiment Video
Updated: Jan 30, 2026

07:41
A Robust Discovery Platform for the Identification of Novel Mediators of Melanoma Metastasis
Published on: March 8, 2022
2.9K
A Self-Assembled ATP Probe for Melanoma Cell Imaging
Hong-Bo Cheng1,2, ZhengWang Sun3, Nahyun Kwon1
1Department of Chemistry and Nano Science, Ewha Womans University, Seoul, 120-750, Korea.
Chemistry (Weinheim an Der Bergstrasse, Germany)
|January 16, 2019
Summary
A novel terpyridine metal complex acts as a sensitive probe for detecting adenosine triphosphate (ATP) and imaging melanoma cells. This probe exhibits a turn-on fluorescence response upon binding with ATP, enabling targeted cellular imaging.
Area of Science:
- Coordination Chemistry
- Biomedical Imaging
- Analytical Chemistry
Background:
- Adenosine triphosphate (ATP) plays crucial roles in cellular processes.
- Melanoma detection and imaging are vital for diagnosis and treatment.
- Development of selective and sensitive probes is essential for biological research.
Purpose of the Study:
- To develop a new terpyridine metal complex as a probe.
- To achieve selective detection of ATP.
- To enable imaging of melanoma cells.
Main Methods:
- Synthesis of a novel terpyridine metal complex.
- Investigation of the complex's interaction with ATP.
- Evaluation of the probe's performance in detecting ATP.
- Application of the probe for imaging melanoma cells.
Main Results:
- The terpyridine metal complex demonstrated selective detection of ATP.
- The complex showed a 'turn-on' fluorescence response upon ATP binding.
- The probe was successfully utilized for imaging melanoma cells.
Conclusions:
- The developed terpyridine metal complex serves as an effective probe for ATP detection.
- This probe facilitates selective imaging of melanoma cells.
- The findings offer a new tool for biomedical research and diagnostics.
Related Concept Videos
ATP Yield
78.9K
Cellular respiration produces 30 - 32 ATP per glucose molecule. Although most of the ATP results from oxidative phosphorylation and the electron transport chain (ETC), 4 ATP are gained beforehand (2 from glycolysis and 2 from the citric acid cycle).
The ETC is embedded in the inner mitochondrial membrane and is comprised of four main protein complexes and an ATP synthase. NADH and FADH2 pass electrons to these complexes, which pump protons into the intermembrane space. This distribution of...
The ETC is embedded in the inner mitochondrial membrane and is comprised of four main protein complexes and an ATP synthase. NADH and FADH2 pass electrons to these complexes, which pump protons into the intermembrane space. This distribution of...
78.9K
Hydrolysis of ATP
81.3K
The bonds of adenosine triphosphate (ATP) can be broken through the addition of water, releasing one or two phosphate groups in an exergonic process called hydrolysis. This reaction liberates the energy in the bonds for use in the cell—for instance, to synthesize proteins from amino acids.
If one phosphate group is removed, a molecule of ADP—adenosine diphosphate—remains, along with inorganic phosphate. ADP can be further hydrolyzed to AMP—adenosine...
If one phosphate group is removed, a molecule of ADP—adenosine diphosphate—remains, along with inorganic phosphate. ADP can be further hydrolyzed to AMP—adenosine...
81.3K
Protein Complex Assembly
16.7K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
16.7K
ATP Synthase: Mechanism
17.1K
In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
17.1K
ATP and Energy Production
1.8K
Adenosine triphosphate (ATP) is a critical molecule that functions as the main energy carrier in cells. Structurally, ATP consists of an adenosine molecule—comprising adenine and ribose—bonded to three phosphate groups. The high-energy bonds between these phosphate groups store significant amounts of potential energy. This energy is released during hydrolysis, wherein ATP is converted to adenosine diphosphate (ADP) or adenosine monophosphate (AMP), driving a variety of essential...
1.8K
Chemiosmosis and ATP Synthesis
2.1K
The electron transport chain is a critical component of cellular respiration, occurring in the inner mitochondrial membrane. It facilitates the transfer of high-energy electrons from reduced cofactors NADH and FADH₂ to molecular oxygen, the final electron acceptor. This transfer of electrons through a series of protein complexes is tightly coupled to the translocation of protons across the membrane, generating a proton gradient essential for ATP synthesis.Electron Flow and Proton...
2.1K

