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Related Concept Videos

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...
Micelles01:30

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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...
Asymmetric Lipid Bilayer01:35

Asymmetric Lipid Bilayer

Biological membranes show uneven distribution of different types of lipids in the inner and outer layers, resulting in transverse asymmetric membranes. The treatment of the erythrocyte membrane with the enzyme phospholipase confirmed the asymmetric nature of the lipid bilayer. The enzyme hydrolyzes lipids into fatty acids and hydrophilic groups. The phospholipase acts only on the outer layer of the membrane, while the inner layer remains intact. The phospholipase treatment resulted in 80%...
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
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Fluid Mosaic Model01:34

Fluid Mosaic Model

The fluid mosaic model was first proposed as a visual representation of research observations. The model comprises the composition and dynamics of membranes and serves as a foundation for future membrane-related studies. The model depicts the structure of the plasma membrane with a variety of components, which include phospholipids, proteins, and carbohydrates. These integral molecules are loosely bound, defining the cell’s border and providing fluidity for optimal function.LipidsThe most...
Fluid Mosaic Model01:19

Fluid Mosaic Model

Scientists identified the plasma membrane in the 1890s and its principal chemical components (lipids and proteins) by 1915. The model for plasma membrane structure, proposed in 1935 by Hugh Davson and James Danielli, was the first model to be widely accepted in the scientific community. The model was based on the plasma membrane's "railroad track" appearance in early electron micrographs. Davson and Danielli theorized that the plasma membrane's structure resembled a sandwich with the analogy of...

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Related Experiment Video

Updated: Jun 27, 2026

Assembly of Cell Mimicking Supported and Suspended Lipid Bilayer Models for the Study of Molecular Interactions
12:18

Assembly of Cell Mimicking Supported and Suspended Lipid Bilayer Models for the Study of Molecular Interactions

Published on: August 3, 2021

Peptide-phospholipid complex formation at liquid-liquid interfaces.

Manuel A Méndez1, Michel Prudent, Bin Su

  • 1Laboratoire d'Electrochimie Physique et Analytique, Ecole Polytechnique Fédérale de Lausanne, Station 6, CH-1015 Lausanne, Switzerland.

Analytical Chemistry
|December 17, 2008
PubMed
Summary
This summary is machine-generated.

Angiotensin III and Leu-enkephalin peptides interact with cell membrane lipids. Electrochemical and mass spectrometry studies reveal complex formation, elucidating peptide-lipid interactions at interfaces.

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PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions
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PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions

Published on: July 27, 2017

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Last Updated: Jun 27, 2026

Assembly of Cell Mimicking Supported and Suspended Lipid Bilayer Models for the Study of Molecular Interactions
12:18

Assembly of Cell Mimicking Supported and Suspended Lipid Bilayer Models for the Study of Molecular Interactions

Published on: August 3, 2021

PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions
10:58

PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions

Published on: July 27, 2017

Area of Science:

  • Biophysical Chemistry
  • Analytical Chemistry
  • Membrane Biophysics

Background:

  • Cell membrane receptors interact with peptides like angiotensin III (Ang III) and Leu-enkephalin (LeuEnk).
  • Understanding peptide-lipid interactions is crucial for cell membrane studies.

Purpose of the Study:

  • To investigate the electrochemical behavior of Ang III and LeuEnk at a liquid-liquid interface modified by a dipalmitoylphosphatidylcholine (DPPC) lipid monolayer.
  • To characterize the formation and stability of peptide-lipid complexes using voltammetry and mass spectrometry.

Main Methods:

  • Electrochemical studies at the interface of two immiscible electrolyte solutions.
  • Voltammetry to determine complexation constants.
  • Biphasic electrospray ionization mass spectrometry (ESI-MS) for complex identification.
  • Temperature-dependent ESI-MS to evaluate complex stability.

Main Results:

  • Cationic Ang III forms a complex with DPPC, facilitating its transfer across the interface, with a complexation constant of 5.2 x 10(4) M(-1).
  • Neutral LeuEnk forms a complex with DPPC, involving lithium cations, which is observable electrochemically.
  • Peptide-lipid complexes were identified and their stability evaluated, revealing a mechanism for peptide-DPPC monolayer interactions.

Conclusions:

  • DPPC monolayers facilitate the interfacial complexation and transfer of Ang III and LeuEnk.
  • Voltammetry and mass spectrometry provide complementary insights into peptide-lipid interactions.
  • The study formulates a mechanism for the interaction between biologically relevant peptides and DPPC monolayers.