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

Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

28.0K
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...
28.0K
Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

3.9K
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...
3.9K

You might also read

Related Articles

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

Sort by
Same author

Goldilocks-Inspired Design of Mid-Size Macrocycles for Selective Targeting of Human Melanocortin Receptors.

Journal of medicinal chemistry·2026
Same author

Reaching Increased Hydrogel Stability <i>In Vivo</i> through β-Hairpin Peptide-Based Hydrogels.

Biomacromolecules·2026
Same author

Endosomal escape and cytosolic delivery of cell-penetrating peptide conjugates.

Bioorganic & medicinal chemistry·2026
Same author

Diverse ring architectures of cyclic peptidomimetics targeting melanocortin receptors.

RSC medicinal chemistry·2026
Same author

The Starting Point for Biomolecular Crystallisation.

Advances in biochemical engineering/biotechnology·2026
Same author

Contact Parallel Cascade Selection Molecular Dynamics (cPaCS-MD) for Accurate In Silico Prediction of Peptide Binding Free Energy.

Journal of chemical information and modeling·2025
Same journal

An intrinsically stretchable nanowire-based sensing patch for wearable analysis of sweat chloride ion composition.

Chemical communications (Cambridge, England)·2026
Same journal

A sterically rigid-flexible balanced NHC-Pd precatalyst for room-temperature solvent-free C-N coupling of benzocyclic amines.

Chemical communications (Cambridge, England)·2026
Same journal

Portable fluorescent conjugated microporous polymer sensor coupled with a smartphone for on-site Fe<sup>3+</sup> detection in water.

Chemical communications (Cambridge, England)·2026
Same journal

Accelerated discovery of NO<sub>3</sub>RR single-atom catalysts <i>via</i> high-throughput DFT and machine learning.

Chemical communications (Cambridge, England)·2026
Same journal

Wafer-scale robust graphene electronics under industrial processing conditions.

Chemical communications (Cambridge, England)·2026
Same journal

Subnanoscale IrW oxide anodes: breaking immiscibility for high activity and durability in water electrolysis.

Chemical communications (Cambridge, England)·2026
See all related articles

Related Experiment Video

Updated: Mar 1, 2026

DNA Nanotubes as a Versatile Tool to Study Semiflexible Polymers
08:00

DNA Nanotubes as a Versatile Tool to Study Semiflexible Polymers

Published on: October 25, 2017

7.3K

Parallel and antiparallel cyclic d/l peptide nanotubes.

Mitchell R Silk1, Janet Newman, Julian C Ratcliffe

  • 1Medicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville, Victoria 3052, Australia. david.chalmers@monash.edu.

Chemical Communications (Cambridge, England)
|June 6, 2017
PubMed
Summary
This summary is machine-generated.

Researchers determined the first crystal structures of cyclic peptide (CP) nanotubes, revealing antiparallel and parallel stacking arrangements. This structural insight advances nanomaterial development from diverse peptide self-assembly.

More Related Videos

Stable DNA Motifs, 1D and 2D Nanostructures Constructed from Small Circular DNA Molecules
09:32

Stable DNA Motifs, 1D and 2D Nanostructures Constructed from Small Circular DNA Molecules

Published on: April 12, 2019

7.2K
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

13.5K

Related Experiment Videos

Last Updated: Mar 1, 2026

DNA Nanotubes as a Versatile Tool to Study Semiflexible Polymers
08:00

DNA Nanotubes as a Versatile Tool to Study Semiflexible Polymers

Published on: October 25, 2017

7.3K
Stable DNA Motifs, 1D and 2D Nanostructures Constructed from Small Circular DNA Molecules
09:32

Stable DNA Motifs, 1D and 2D Nanostructures Constructed from Small Circular DNA Molecules

Published on: April 12, 2019

7.2K
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

13.5K

Area of Science:

  • Supramolecular chemistry
  • Nanomaterials science
  • Structural biology

Background:

  • Hydrogen-bonded cyclic peptide (CP) nanotubes offer potential for diverse nanomaterials.
  • Structural characterization challenges have limited the development of these CP nanotubes.

Purpose of the Study:

  • To present the first crystal structures of continuous cyclic peptide nanotubes.
  • To elucidate the distinct antiparallel and parallel stacking arrangements in CP nanotubes.

Main Methods:

  • X-ray crystallography was employed to determine the structures.
  • Two specific cyclic peptides, cyclo[(Asp-d-Leu-Lys-d-Leu)2] and cyclo[(Asp-d-Ala-Lys-d-Ala)2], were synthesized and assembled into nanotubes.

Main Results:

  • The first crystal structures of continuous cyclic peptide nanotubes were obtained.
  • Two distinct stacking arrangements were identified: antiparallel and parallel.
  • The structures were determined for nanotubes assembled from cyclo[(Asp-d-Leu-Lys-d-Leu)2] and cyclo[(Asp-d-Ala-Lys-d-Ala)2].

Conclusions:

  • This work provides crucial structural insights into cyclic peptide nanotube assembly.
  • Understanding these stacking arrangements facilitates the rational design of novel peptide-based nanomaterials.