Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

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.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Small RNAs, big potential: Engineering microRNA-based synthetic gene circuits.

Current opinion in chemical biology·2026
Same author

Repurposing nuclear receptors for ligand-responsive liquid condensate formation and gene regulation.

Nature communications·2026
Same author

Self-assembling protein cages: from coiled-coil module to machine learning-driven <i>de novo</i> design of next-generation biomaterials.

Materials advances·2025
Same author

Structural flexibility of a recombinant intrinsically disordered LEA protein from Ramonda serbica.

Scientific reports·2025
Same author

RNA <i>trans</i>-splicing to rescue β-catenin: A novel approach for treating CTNNB1-Haploinsufficiency disorder.

Molecular therapy. Nucleic acids·2025
Same author

Engineering chimeric PCSK9 for a vaccine against atherosclerosis.

Molecular therapy. Methods & clinical development·2025
Same journal

TDP-43 proteinopathy as a biomarker and therapeutic target in amyotrophic lateral sclerosis.

Biochemical Society transactions·2026
Same journal

Advancing the monitoring of organelle contact sites in vitro and in vivo.

Biochemical Society transactions·2026
Same journal

Mechanisms influencing transient cytoplasmic protein targeting to intracellular lipid droplets.

Biochemical Society transactions·2026
Same journal

Replication associated nuclear DNA mismatch repair across kingdoms.

Biochemical Society transactions·2026
Same journal

Phosphatases of regenerating liver downregulate PTEN to promote tumorigenesis.

Biochemical Society transactions·2026
Same journal

Implications of Rho GTPase signaling in cancer immunotherapy.

Biochemical Society transactions·2026
See all related articles

Related Experiment Video

Updated: May 20, 2026

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

Functional self-assembling polypeptide bionanomaterials.

Tibor Doles1, Sabina Božič, Helena Gradišar

  • 1Department of Biotechnology, National Institute of Chemistry, Ljubljana, Slovenia.

Biochemical Society Transactions
|July 24, 2012
PubMed
Summary
This summary is machine-generated.

This review explores bionanomaterials made from polypeptides, focusing on self-assembly for creating nanoscale pores. These materials offer tunable properties for advanced separation applications.

More Related Videos

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly
09:34

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

Published on: February 6, 2020

Fabrication and Characterization of Colorectal Cancer Organoids from SW1222 Cell Line in Ultrashort Self&#45;Assembling Peptide Matrix
10:23

Fabrication and Characterization of Colorectal Cancer Organoids from SW1222 Cell Line in Ultrashort Self-Assembling Peptide Matrix

Published on: May 3, 2024

Related Experiment Videos

Last Updated: May 20, 2026

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

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly
09:34

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

Published on: February 6, 2020

Fabrication and Characterization of Colorectal Cancer Organoids from SW1222 Cell Line in Ultrashort Self&#45;Assembling Peptide Matrix
10:23

Fabrication and Characterization of Colorectal Cancer Organoids from SW1222 Cell Line in Ultrashort Self-Assembling Peptide Matrix

Published on: May 3, 2024

Area of Science:

  • Bionanotechnology
  • Materials Science
  • Biochemistry

Background:

  • Bionanotechnology utilizes biological systems for nanomaterial production.
  • Molecular self-assembly, a core biological principle, drives artificial bionanomaterial assembly.
  • Protein domains and peptides are ideal building blocks for complex 3D structures.

Purpose of the Study:

  • To review polypeptide-based materials for creating nanometer-scale pores.
  • To explore the application of these materials in separation technologies.
  • To highlight the design principles for tunable bionanomaterials.

Main Methods:

  • Utilizing protein domains and peptides as self-assembling units.
  • Employing antiparallel coiled-coil dimerization domains for pore modulation.
  • Investigating external signal-regulated assembly and disassembly.

Main Results:

  • Polypeptide-based materials can form structures with nanometer-scale pores.
  • Antiparallel coiled-coil domains allow modulation of pore size and chemical properties.
  • External signals, like coumermycin-induced dimerization, can control bionanomaterial assembly.

Conclusions:

  • Polypeptide self-assembly offers a versatile platform for designing functional bionanomaterials.
  • Tunable nanostructured materials have significant potential in separation science.
  • Controllable assembly/disassembly expands the application scope of bionanomaterials.