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Related Concept Videos

Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

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...
Fibril-associated Collagen01:11

Fibril-associated Collagen

Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
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Formation of Intermediate Filaments00:57

Formation of Intermediate Filaments

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 reported.
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...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Complementary π-π interactions induce multicomponent coassembly into functional fibrils.

Derek M Ryan1, Todd M Doran, Bradley L Nilsson

  • 1Department of Chemistry, University of Rochester, Rochester, New York 14627-0216, USA.

Langmuir : the ACS Journal of Surfaces and Colloids
|August 6, 2011
PubMed
Summary
This summary is machine-generated.

Researchers developed sophisticated noncovalent materials by coassembling phenylalanine derivatives. Complementary π-π interactions enabled the formation of novel two-component fibrils and hydrogels for advanced biomedical applications.

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Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly
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Area of Science:

  • Supramolecular Chemistry
  • Materials Science
  • Biomedical Engineering

Background:

  • Noncovalent self-assembled materials mimic amyloid structures for biomedical uses.
  • Developing sophisticated multicomponent fibrils requires selective coassembly of monomers.

Purpose of the Study:

  • To explore the use of complementary π-π interactions for coassembling phenylalanine derivatives.
  • To create novel two-component fibrils and hydrogels with enhanced properties.

Main Methods:

  • Coassembly of Fmoc-Phe and Fmoc-F(5)-Phe derivatives.
  • Investigating coassembly with monohalogenated Fmoc-Phe derivatives (F, Cl, Br).
  • Characterization of formed fibrils and hydrogels.

Main Results:

  • Equimolar mixtures of Fmoc-Phe and Fmoc-F(5)-Phe formed two-component fibrils and hydrogels.
  • Fmoc-Phe alone did not self-assemble under tested conditions.
  • Coassembly was also observed with monohalogenated Fmoc-Phe derivatives, indicating subtle π-π effects.

Conclusions:

  • Complementary π-π interactions are effective for coassembling distinct monomeric units into ordered fibrils.
  • This strategy expands the toolkit for designing advanced noncovalent materials.
  • The findings pave the way for new applications in regenerative medicine and drug delivery.