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Related Concept Videos

Micelles01:30

Micelles

Micelle formation is an intricate process that hinges on the properties of amphiphilic or amphipathic molecules and the conditions of the system in which they are found. Amphiphilic molecules, which have both hydrophilic (water-attracting) and hydrophobic (water-repelling) parts, play a critical role in this process.In aqueous environments, these molecules arrange themselves such that their hydrophilic heads are turned towards the water phase, while their hydrophobic tails are oriented away...
Intermolecular Forces03:13

Intermolecular Forces

Atoms and molecules interact through bonds (or forces): intramolecular and intermolecular. The forces are electrostatic as they arise from interactions (attractive or repulsive) between charged species (permanent, partial, or temporary charges) and exist with varying strengths between ions, polar, nonpolar, and neutral molecules. The different types of intermolecular forces are ion–dipole, dipole–dipole, hydrogen bonds, and dispersion; among these, dipole–dipole, hydrogen bonds, and dispersion...
Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
Detergent Purification of Membrane Proteins01:18

Detergent Purification of Membrane Proteins

Detergents are used to purify the integral proteins of the membrane. The hydrophobic portion of the detergent can replace membrane phospholipids while solubilizing the membrane proteins. When detergent monomers reach a specific concentration in a solution called critical micelle concentration (CMC), they form micelles. Above CMC, the concentration of the detergent monomers remains in equilibrium with the micelle. The number of detergent monomers present in the CMC varies for each detergent, and...
Protein-protein Interfaces02:04

Protein-protein Interfaces

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 polypeptide...

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Contrast-Matching Detergent in Small-Angle Neutron Scattering Experiments for Membrane Protein Structural Analysis and Ab Initio Modeling
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Electrostatic interactions between a protein and oppositely charged micelles.

Patrizia Andreozzi1, Adalberto Bonincontro, Camillo La Mesa

  • 1Dipartimento di Chimica, SOFT-INFM-CNR Research Center, La Sapienza University, Rome, Italy.

The Journal of Physical Chemistry. B
|February 28, 2008
PubMed
Summary

Fully fluorinated surfactant LiPFN forms water-soluble complexes with lysozyme, stabilized by electrostatic and double-layer interactions. These protein-micelle complexes retain a negative charge, with size, charge, and double-layer thickness interrelated.

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Area of Science:

  • Physical Chemistry
  • Biophysics
  • Materials Science

Background:

  • Micellar solutions are crucial in various applications, including drug delivery and biomaterial science.
  • Understanding protein-surfactant interactions is key to controlling complex formation and stability.
  • Fully fluorinated surfactants offer unique properties for forming stable complexes.

Purpose of the Study:

  • To investigate the formation and properties of water-soluble complexes between a fully fluorinated surfactant (LiPFN) and lysozyme.
  • To elucidate the stabilization mechanisms, including electrostatic and double-layer interactions.
  • To develop a model for quantifying the properties of these protein-micelle complexes.

Main Methods:

  • Electrophoretic mobility measurements to determine surface charge density.
  • Dynamic Light Scattering (DLS) to infer changes in particle size.
  • Dielectric relaxation spectroscopy to analyze double-layer thickness.

Main Results:

  • LiPFN micellar solutions form stable, water-soluble complexes with lysozyme across a broad concentration range.
  • Protein-micelle complexes exhibit incomplete charge neutralization, retaining a net negative charge.
  • Interrelationships were observed between particle size, surface charge density, and double-layer thickness.

Conclusions:

  • Electrostatic and double-layer interactions are primary stabilizers of lysozyme-LiPFN complexes.
  • The developed model successfully quantifies the properties of these complexes.
  • Findings provide insights into protein-surfactant complexation for potential applications.