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Related Concept Videos

Mechanism of Lamellipodia Formation01:31

Mechanism of Lamellipodia Formation

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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...
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Mechanism of Filopodia Formation01:39

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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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Actin Polymerization01:42

Actin Polymerization

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Actin polymerization occurs through the head-to-tail association of binding sites on monomeric actin or G-actin to form filamentous or F-actin. The polymerization can be divided into three phases ̶  nucleation, elongation, and steady-state phase.
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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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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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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
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Self-Assembly into Strands in Amphiphilic Polymer Brushes.

Daniil E Larin1, Alexei A Lazutin2, Elena N Govorun1

  • 1Faculty of Physics, M. V. Lomonosov Moscow State University , Leninskie gory, Moscow 119991, Russia.

Langmuir : the ACS Journal of Surfaces and Colloids
|June 9, 2016
PubMed
Summary

Amphiphilic macromolecules grafted to surfaces self-assemble into ordered strands. This self-assembly, driven by monomer amphiphilicity, forms a 2D hexagonal structure influenced by side group length and grafting density.

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Area of Science:

  • Polymer Science
  • Surface Chemistry
  • Materials Science

Background:

  • Amphiphilic macromolecules exhibit unique self-assembly properties.
  • Surface-grafted polymer brushes are relevant in various applications.
  • Understanding self-assembly in confined geometries is crucial.

Purpose of the Study:

  • To investigate the self-assembly behavior of amphiphilic macromolecules end-grafted to a planar surface.
  • To elucidate the structural organization and driving forces behind this self-assembly.
  • To explore the influence of molecular architecture and solvent conditions.

Main Methods:

  • Mean-field theory was employed to model the system.
  • Computer simulations, specifically molecular dynamics (MD), were utilized for detailed analysis.
  • Analysis focused on the local brush structure and overall organization.

Main Results:

  • Strong monomer-level amphiphilicity drives self-assembly into ordered strands.
  • A 2D hexagonal order was observed in cross-sections parallel to the grafting plane.
  • The structure period is dictated by the length of the hydrophilic side groups.
  • Aggregation number of strands increases with grafting density and side group length.

Conclusions:

  • The self-assembly results in a stable, ordered structure due to effective negative surface tension contributions.
  • Molecular dynamics simulations confirm theoretical predictions and provide detailed structural insights.
  • Grafting density and side group length are key parameters controlling the self-assembled morphology.