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Related Concept Videos

Extraction: Advanced Methods00:56

Extraction: Advanced Methods

Metal ions can be separated from one another by complexation with organic ligands–the chelating agent– to form uncharged chelates. Here, the chelating agent must contain hydrophobic groups and behave as a weak acid, losing a proton to bind with the metal. Since most organic ligands used in this process are insoluble or undergo oxidation in the aqueous phase, the chelating agent is initially added to the organic phase and extracted into the aqueous phase. The metal-ligand complex is formed in...
Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
Complexation Equilibria: The Chelate Effect01:19

Complexation Equilibria: The Chelate Effect

In complexation reactions, metal atoms or cations interact with ligands to form donor-acceptor adducts called metal complexes. Ligands that bind through one donor site are monodentate, ligands with two donor sites are bidentate, and those with more than two donor sites are polydentate ligands. For example, ethylene diamine is a bidentate ligand that binds through two nitrogen donor atoms, forming a five-membered ring. EDTA is a polydentate ligand that binds through four oxygen and two nitrogen...
Formation of Complex Ions03:45

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A type of Lewis acid-base chemistry involves the formation of a complex ion (or a coordination complex) comprising a central atom, typically a transition metal cation, surrounded by ions or molecules called ligands. These ligands can be neutral molecules like H2O or NH3, or ions such as CN− or OH−. Often, the ligands act as Lewis bases, donating a pair of electrons to the central atom. These types of Lewis acid-base reactions are examples of a broad subdiscipline called coordination...
Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

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Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
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Related Experiment Video

Updated: May 22, 2026

Quantifying the Binding Interactions Between Cu(II) and Peptide Residues in the Presence and Absence of Chromophores
11:38

Quantifying the Binding Interactions Between Cu(II) and Peptide Residues in the Presence and Absence of Chromophores

Published on: April 5, 2022

Phosphatidylserine reversibly binds Cu2+ with extremely high affinity.

Christopher F Monson1, Xiao Cong, Aaron D Robison

  • 1Department of Chemistry, Texas A&M University, 3255 TAMU, College Station, Texas 77843, USA.

Journal of the American Chemical Society
|May 3, 2012
PubMed
Summary

Phosphatidylserine (PS) binds copper ions (Cu2+) with extremely high affinity. This interaction quenches fluorescent signals reversibly, depending on pH and copper concentration.

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Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

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Last Updated: May 22, 2026

Quantifying the Binding Interactions Between Cu(II) and Peptide Residues in the Presence and Absence of Chromophores
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Published on: April 5, 2022

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

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Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides
11:04

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

Published on: September 7, 2019

Area of Science:

  • Biochemistry
  • Biophysics
  • Materials Science

Background:

  • Phosphatidylserine (PS) is a key phospholipid in cell membranes.
  • Copper ions (Cu2+) play crucial roles in biological systems.
  • Interactions between lipids and metal ions are vital for cellular processes.

Purpose of the Study:

  • To investigate the binding affinity of Cu2+ to PS in supported lipid bilayers.
  • To characterize the complex formed between Cu2+ and PS.
  • To explore the functional consequences of this interaction, including fluorescence quenching.

Main Methods:

  • Utilized supported lipid bilayers incorporating phosphatidylserine.
  • Measured Cu2+ binding affinity using equilibrium dissociation constants.
  • Assessed fluorescence quenching of lipid-bound fluorophores.
  • Investigated pH-dependent behavior and reaction kinetics.

Main Results:

  • PS binds Cu2+ with femtomolar affinity, forming a 1:2 Cu2+-to-PS complex.
  • The complex reversibly quenches lipid-bound fluorophores in a pH-dependent manner (pH 5-8).
  • Quenching is significant at basic pH (85-90%) and diminishes at acidic pH.
  • Binding kinetics are slow at basic pH and rapid dissociation occurs at acidic pH.

Conclusions:

  • Cu2+ exhibits exceptionally high affinity for PS in lipid bilayers.
  • The Cu2+-PS interaction modulates fluorescence, offering potential sensing applications.
  • The pH-dependent nature suggests physiological relevance in certain cellular environments.