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Related Concept Videos

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.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...
Mechanisms of Membrane-bending01:15

Mechanisms of Membrane-bending

The living membranes are flexible due to their fluid mosaic nature; however, their bending into different shapes is an active process regulated by specific lipids and proteins. The membrane bending can be transient as seen in vesicles or stable for a long time as in microvilli. Cells regulate the size, location, and duration of the membrane curvature.
Membrane bending can happen due to intrinsic changes in lipid composition or extrinsic association with different proteins. The proteins involved...
Potentiometry: Membrane Electrodes01:15

Potentiometry: Membrane Electrodes

Membrane electrodes, also known as p-ion electrodes, use membranes that selectively interact with free analyte ions, generating a potential difference across the membrane. The resulting membrane potential, known as the asymmetry potential, is not zero even when analyte concentrations on both sides of the membrane are equal. The membrane's response is typically not selective to a single analyte but proportional to the concentration of all ions in the sample solution capable of interacting at the...
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...
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
Membrane Domains01:18

Membrane Domains

The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the anterior...

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Updated: May 8, 2026

In Vitro Reconstitution of Self-Organizing Protein Patterns on Supported Lipid Bilayers
08:10

In Vitro Reconstitution of Self-Organizing Protein Patterns on Supported Lipid Bilayers

Published on: July 28, 2018

Electrostatic control of structure in self-assembled membranes.

Ronit Bitton1, Lesley W Chow, R Helen Zha

  • 1Institute for BioNanotechnology in Medicine, Northwestern University, Chicago, IL, 60611, USA.

Small (Weinheim an Der Bergstrasse, Germany)
|September 12, 2013
PubMed
Summary

Self-assembling peptide amphiphiles form ordered membranes through interfacial aggregation. This process is crucial for creating diffusion barriers and templating nanofiber growth, leading to hierarchical structures.

Keywords:
SAXSordered membranespeptide amphiphilespolyelectrolyte-supramolecular polymer complexself-assembly

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Published on: May 1, 2020

Area of Science:

  • Materials Science
  • Biomaterials Engineering
  • Nanotechnology

Background:

  • Self-assembling peptide amphiphiles (PAs) are versatile building blocks for creating nanostructured materials.
  • Formation of ordered membranes from PAs typically involves interactions with oppositely charged polyelectrolytes.
  • Hierarchical self-assembly is a key process for developing advanced functional materials.

Purpose of the Study:

  • To investigate the role of interfacial aggregation in the hierarchical self-assembly of peptide amphiphile membranes.
  • To explore how varying polyelectrolyte charge density influences PA aggregation and membrane formation.
  • To understand the nanoscale structural organization within peptide amphiphile membranes formed under different interaction strengths.

Main Methods:

  • Utilized heparin-binding peptide amphiphiles (PAs) and interacted them with heparin and other polyelectrolytes.
  • Employed small-angle X-ray scattering (SAXS) to analyze the nanoscale structure of the formed membranes.
  • Investigated the impact of polyelectrolyte charge density on PA aggregation and membrane morphology.

Main Results:

  • Massive interfacial aggregation of PA molecules is essential for hierarchical membrane formation.
  • Rapid diffusion barrier formation, driven by PA aggregation, precedes templated nanofiber growth.
  • Weak PA-polyelectrolyte interactions resulted in membranes with cubic phase ordering at the nanoscale.
  • Stronger interactions promoted the formation of filamentous nanostructures parallel to the membrane plane.

Conclusions:

  • Hierarchical membrane formation by peptide amphiphiles is critically dependent on significant interfacial aggregation.
  • The strength of PA-polyelectrolyte interactions dictates the resulting nanoscale structure, ranging from cubic phases to filamentous arrays.
  • Understanding these self-assembly principles enables the rational design of peptide amphiphile-based nanomaterials with tunable properties.