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Related Concept Videos

Mechanism of Lamellipodia Formation01:31

Mechanism of Lamellipodia Formation

Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...
Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin networks...
Actin Filament Depolymerization01:19

Actin Filament Depolymerization

Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
In F-actin, the ADF/cofilin proteins...

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Related Experiment Video

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Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles
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A self-assembly pathway to aligned monodomain gels.

Shuming Zhang1, Megan A Greenfield, Alvaro Mata

  • 1Department of Materials Science and Engineering, Northwestern University, Evanston, Illinois 60208, USA.

Nature Materials
|June 15, 2010
PubMed
Summary

Charged amphiphilic molecules form aligned nanoscale fibers at high temperatures. These fibers can be assembled into centimeter-long cellular wires for biological applications.

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Area of Science:

  • Supramolecular chemistry
  • Materials science
  • Biotechnology

Background:

  • Charged amphiphilic molecules self-assemble into complex structures.
  • Temperature-induced phase transitions can alter molecular organization.
  • Controlling nanoscale alignment is crucial for advanced materials.

Purpose of the Study:

  • To investigate the temperature-induced structural transitions of charged amphiphilic molecule aggregates.
  • To explore methods for macroscopic alignment of supramolecular fibrils.
  • To develop biocompatible cellular wires using self-assembled materials.

Main Methods:

  • Thermal treatment of charged amphiphilic molecule aggregates.
  • Macroscopic alignment via extrusion of liquid crystalline phase.
  • Mixing with cells at physiological temperatures to form gels.

Main Results:

  • A lamellar plaque structure forms at elevated temperatures, templating fibril alignment.
  • Cooling yields aligned nanoscale fibers and a birefringent liquid.
  • Extrusion creates centimeter-scale viscoelastic strings of aligned fibers.
  • Formation of monodomain gels with aligned cells and filaments.

Conclusions:

  • Self-assembly of charged amphiphiles provides a pathway to macroscopic alignment.
  • The process is biocompatible, enabling in situ formation of cellular wires.
  • Customizable peptide compositions allow for tailored biological applications.