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Related Concept Videos

Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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The hemoglobin in the blood, the chlorophyll in green plants, vitamin B-12, and the catalyst used in the manufacture of polyethylene all contain coordination compounds. Ions of the metals, especially the transition metals, are likely to form complexes.
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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...
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Essential proteins such as insulin or low-density lipoprotein (LDL) and micronutrients such as iron enter a eukaryotic cell through receptor-mediated endocytosis. Subsequently, the early endosomes fuse with the vesicles containing such receptor-ligand complexes and play a vital role in sorting the incoming ligands and receptors. While the ligands are either degraded inside the vesicle or released into the cytosol, their receptors are returned to the plasma membrane for further rounds of...
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The Equilibrium Binding Constant and Binding Strength02:18

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The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
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Protein-protein Interfaces

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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Related Experiment Video

Updated: Dec 18, 2025

Synthetic Methodology for Asymmetric Ferrocene Derived Bio-conjugate Systems via Solid Phase Resin-based Methodology
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Double-Interface Binding of Two Bioactive Compounds with Cage-Like Ferritin.

Demei Meng1, Shengnan Chen1, Jie Liu2

  • 1State Key Laboratory of Food Nutrition and Safety, College of Food Science and Engineering, Tianjin University of Science and Technology, Tianjin 300457, People's Republic of China.

Journal of Agricultural and Food Chemistry
|June 18, 2020
PubMed
Summary

Researchers modified ferritin, a protein cage, with hesperetin to create a nanocarrier. This hesperetin covalently modified ferritin (HFRT) successfully encapsulated quercetin, enhancing its stability for potential food applications.

Keywords:
encapsulationferritinhesperetinnanocarrierstability

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Area of Science:

  • Biomaterials Science
  • Nanotechnology
  • Protein Engineering

Background:

  • Ferritin is a natural cage-like protein capable of carrying molecules.
  • Modifying ferritin's surface can create novel nanocarriers.
  • Bioactive compounds like hesperetin and quercetin have health benefits but require stable delivery.

Purpose of the Study:

  • To covalently conjugate hesperetin to the outer surface of ferritin.
  • To encapsulate quercetin within the modified ferritin structure.
  • To evaluate the stability and functional properties of the novel nanocarrier for food applications.

Main Methods:

  • Covalent conjugation of hesperetin to ferritin at pH 9.0.
  • Characterization of hesperetin covalently modified ferritin (HFRT) structure and binding.
  • pH-regulated self-assembly for inner surface encapsulation of quercetin.
  • Assessment of HFRT's digestive and thermal stability compared to unmodified ferritin.

Main Results:

  • Hesperetin was successfully conjugated to ferritin with a binding of 12.33 ± 0.56 nmol/mg.
  • HFRT retained ferritin's cage structure and exhibited pH-dependent reversible self-assembly.
  • Quercetin was encapsulated into HFRT with a 14.0 ± 1.36% (w/w) encapsulation ratio.
  • Hesperetin modification enhanced ferritin's digestive stability and quercetin's thermal stability.

Conclusions:

  • Ferritin can be functionalized on both its inner and outer surfaces with different bioactive compounds.
  • Hesperetin modification improves ferritin's stability and creates a robust nanocarrier for quercetin.
  • This dual-functionalized ferritin holds promise as a nanocarrier in food applications.