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

21.2K
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...
21.2K
Aquaporins01:25

Aquaporins

4.9K
Aquaporins or AQPs are a family of integral membrane proteins whose primary function is to transport water, while some called aquaglyceroporins also transport glycerol. In addition, aquaporins have also been suspected to be involved in transporting volatile substances, such as carbon dioxide and ammonia, across membranes. Such AQPs that act as gas channels are often highly expressed in cells involved in the gaseous exchange, such as red blood cells, epithelial cells, and pulmonary capillaries.
4.9K
Peptide Bonds02:43

Peptide Bonds

75.1K
A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
75.1K
Protein Organization01:13

Protein Organization

139.0K
Overview
139.0K
Protein Folding01:22

Protein Folding

118.7K
Overview
118.7K

You might also read

Related Articles

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

Sort by
Same author

Oppositely-charged coordination cages form a type I porous ionic liquid with two pore sizes.

Materials horizons·2026
Same author

Peptide cages: bioinspired supramolecular architectures for next-generation applications.

Chemical science·2026
Same author

Dual pH-responsive pseudopeptide: hydrogelation and self-assembly into single- and multi-walled nanotubes.

Nanoscale·2026
Same author

A Dynamic Silver(I) Nanocluster Holds Together a 3 × 3 Self-Assembled Grid.

Journal of the American Chemical Society·2025
Same author

Characterising supramolecular gels: general discussion.

Faraday discussions·2025
Same author

Using supramolecular gels: general discussion.

Faraday discussions·2025

Related Experiment Video

Updated: Aug 10, 2025

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

13.0K

Nanotubes and water-channels from self-assembling dipeptides.

Ottavia Bellotto1, Paola D'Andrea2, Silvia Marchesan1,3

  • 1Chem. Pharm. Sc. Dept., University of Trieste, Via Giorgieri 1, 34127 Trieste, Italy. smarchesan@units.it.

Journal of Materials Chemistry. B
|February 15, 2023
PubMed
Summary
This summary is machine-generated.

Dipeptides like diphenylalanine self-assemble into nanotubes, offering biocompatible building blocks for advanced biomaterials. Further research explores design rules for creating these nanostructures for diverse applications.

More Related Videos

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid
10:42

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid

Published on: February 27, 2019

9.5K
Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures
08:15

Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures

Published on: June 26, 2020

4.3K

Related Experiment Videos

Last Updated: Aug 10, 2025

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

13.0K
A Tripeptide-Stabilized Nanoemulsion of Oleic Acid
10:42

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid

Published on: February 27, 2019

9.5K
Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures
08:15

Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures

Published on: June 26, 2020

4.3K

Area of Science:

  • Biomaterials Science
  • Nanotechnology
  • Supramolecular Chemistry

Background:

  • Dipeptides are increasingly recognized for their biocompatibility and biodegradability, making them promising for biomaterials.
  • Diphenylalanine (Phe-Phe) nanotubes demonstrated the potential of dipeptides in forming nanostructures.
  • Predictive design rules for dipeptide nanotube formation remain largely undiscovered.

Purpose of the Study:

  • To review known dipeptide sequences capable of forming nanotubes.
  • To analyze the structural properties and formation mechanisms of these dipeptide nanotubes.
  • To explore the potential biological applications of dipeptide-based nanostructures.

Main Methods:

  • Literature review of dipeptide sequences reported to form nanotubes.
  • Analysis of structural data, including single-crystal X-ray diffraction, to understand nanotube morphology.
  • Compilation of reported properties and applications of dipeptide nanotubes.

Main Results:

  • Identified various dipeptide sequences that self-assemble into nanotubes.
  • Observed that many dipeptide nanotubes possess water-filled supramolecular channels.
  • Documented a wide range of potential applications, including drug delivery, regenerative medicine, bioelectronics, and bioimaging.

Conclusions:

  • Dipeptides are versatile building blocks for creating nanotubular biomaterials.
  • Understanding the structure-property-application relationships of dipeptide nanotubes is crucial.
  • Dipeptide nanotubes hold significant promise for diverse biomedical and technological applications.