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Related Concept Videos

Formation of Intermediate Filaments00:57

Formation of Intermediate Filaments

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Intermediate filaments are cytoskeletal proteins with higher tensile strength and flexibility than microfilaments and microtubules. Unlike the other two cytoskeletal proteins, intermediate filament formation lacks the enzymatic activity to hydrolyze nucleotides like ATP and GTP to generate energy for polymerization. Therefore, the formation of intermediate filaments is multistep self-assembly. The involvement of any accessory proteins in intermediate filament formation has not yet been...
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Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

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Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
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The Structure of Intermediate Filaments01:19

The Structure of Intermediate Filaments

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The intermediate filaments are one of three widely studied cytoskeletal filaments. They are so named as their diameter (10 nm) is in between that of microfilaments (7 nm) and the microtubules (25 nm).  These filaments are highly stable and can remain intact when exposed to high salt concentrations and detergents. These filaments are responsible for providing stability and mechanical support to the cells. They also help in cell adhesion and maintaining tissue integrity.
Intermediate...
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Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

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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...
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Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

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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...
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Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

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The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
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ECM Protein Nanofibers and Nanostructures Engineered Using Surface-initiated Assembly
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Self-Assembled Molecular Fibers Aligned by Compression in Water.

Norihiro Mizoshita1, Yuri Yamada1, Yumi Masuoka1

  • 1Toyota Central R&D Labs., Inc., Nagakute, Aichi, 480-1192, Japan.

Small (Weinheim an Der Bergstrasse, Germany)
|April 29, 2024
PubMed
Summary

Researchers developed a compression technique to align self-assembled molecular nanofibers into bundles. This method enables the creation of vertically oriented porous membranes, overcoming challenges in industrial nanostructure manufacturing.

Keywords:
compressionhydrophobic interactionsnanofibersorganosilicasphysical gelsself‐assembly

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Area of Science:

  • Materials Science
  • Nanotechnology
  • Chemical Engineering

Background:

  • Molecular self-assembly offers energy-efficient fabrication of nano-objects like nanofibers and nanotubes.
  • Industrial application of molecular self-assembly is hindered by difficulties in controlling product position and direction.
  • Self-assembled molecular structures are often too fragile for mechanical handling.

Purpose of the Study:

  • To demonstrate a method for macroscopic alignment of self-assembled molecular fibers.
  • To overcome the limitations of fragility and directional control in self-assembled nanostructures.
  • To develop a scalable technique for producing nanostructured functional materials.

Main Methods:

  • Macroscopic alignment of self-assembled molecular fibers using compression.
  • Dispersion of self-assembled nanofibers in water to achieve macroscopic bundling.
  • Chemical crosslinking of fiber bundles using trialkoxysilyl groups.
  • Rapid production of vertically oriented porous membranes by slicing fiber bundles.

Main Results:

  • Successful macroscopic alignment and bundling of self-assembled nanofibers via compression.
  • Chemically crosslinked fiber bundles maintained morphology without significant changes.
  • Vertically oriented porous membranes were rapidly produced from the aligned fiber bundles.
  • Demonstrated a viable method for handling and processing fragile self-assembled nanostructures.

Conclusions:

  • Compression-induced alignment offers a scalable approach for manipulating self-assembled molecular fibers.
  • The developed technique facilitates the production of anisotropic nanostructured materials, such as porous membranes.
  • This method holds promise for advancing the industrial manufacturing of functional nanomaterials.