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

Semiconductors01:22

Semiconductors

1.6K
There is variation in the electrical conductivity of materials - metals, semiconductors, and insulators that are showcased with the help of the energy band diagrams.
Metals such as copper (Cu), zinc (Zn), or lead (Pb) have low resistivity and feature conduction bands that are either not fully occupied or overlap with the valence band, making a bandgap non-existent. This allows electrons in the highest energy levels of the valence band to easily transition to the conduction band upon gaining...
1.6K
Protein Complex Assembly02:41

Protein Complex Assembly

16.9K
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...
16.9K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

6.7K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
6.7K
Peptide Bonds02:43

Peptide Bonds

83.8K
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...
83.8K

You might also read

Related Articles

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

Sort by
Same author

Reprogramming Chirality in Peptide Self-Assembly via Intramolecular Side Chain-Backbone Hydrogen Bonding.

Nano letters·2026
Same author

Self-Assembly Behavior of Amino Acids on Au (111) Surfaces: A Molecular Dynamics Study.

Langmuir : the ACS journal of surfaces and colloids·2026
Same author

Formation of S- and Z-twist supramolecular micro-ropes by peptide stereoisomers.

Nature communications·2026
Same author

CO<sub>2</sub> Conversion by a Metal-Coordinated Single Amino Acid Carbonic Anhydrase Enzyme Mimic.

ACS applied materials & interfaces·2026
Same author

Amyloid-β "Co-assembles" with Coatomer Subunit Delta (δ-COP).

The journal of physical chemistry letters·2026
Same author

Shikimate pathway disruption in yeast induces metabolite self-assembly into toxic aggregates.

The FEBS journal·2026
Same journal

Erratum for the Research Article "Detecting supramolecular organic nanoparticles during heat wave".

Science (New York, N.Y.)·2026
Same journal

Local signals, systemic decline.

Science (New York, N.Y.)·2026
Same journal

The mechanics of liver regeneration.

Science (New York, N.Y.)·2026
Same journal

Computing in a memory with physics.

Science (New York, N.Y.)·2026
Same journal

Retraction.

Science (New York, N.Y.)·2026
Same journal

Making time.

Science (New York, N.Y.)·2026
See all related articles

Related Experiment Video

Updated: Feb 18, 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

13.5K

Self-assembling peptide semiconductors.

Kai Tao1, Pandeeswar Makam1, Ruth Aizen1

  • 1Department of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 6997801, Israel.

Science (New York, N.Y.)
|November 18, 2017
PubMed
Summary
This summary is machine-generated.

Peptide self-assemblies offer a novel route to creating durable, bioinspired nanoscale semiconductors. These materials exhibit tunable semiconducting properties, potentially bridging inorganic electronics and biological systems.

More Related Videos

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid
10:42

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid

Published on: February 27, 2019

9.9K
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

8.0K

Related Experiment Videos

Last Updated: Feb 18, 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

13.5K
A Tripeptide-Stabilized Nanoemulsion of Oleic Acid
10:42

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid

Published on: February 27, 2019

9.9K
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

8.0K

Area of Science:

  • Materials Science
  • Nanotechnology
  • Biophysics

Background:

  • Conventional semiconductors face limitations in bio-interfacing and nanoscale fabrication.
  • Peptide self-assemblies present a promising alternative for advanced semiconductor applications.

Purpose of the Study:

  • To explore the potential of peptide self-assemblies as nanoscale semiconductors.
  • To investigate the mechanisms underlying their semiconducting properties and tunability.

Main Methods:

  • Utilizing self-assembled nanostructures formed by short peptides.
  • Analyzing intermolecular interactions (π-π stacking, hydrogen bonding) driving self-assembly.
  • Characterizing quantum confinement effects and band gap reduction.

Main Results:

  • Peptide self-assemblies form highly ordered structures with quantum confinement.
  • Band gaps are reduced into the semiconductor range due to these structures.
  • Semiconductivity is tunable, dopeable, and functionalizable via peptide architecture.

Conclusions:

  • Electroactive supramolecular peptide materials offer a pathway to bioinspired semiconductors.
  • These materials can potentially interface inorganic electronics with biological systems.
  • Peptide self-assemblies provide a versatile platform for next-generation electronic and optical devices.