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

17.1K
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...
17.1K
Protein Folding01:25

Protein Folding

12.7K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
12.7K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

7.2K
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,...
7.2K
Metal-Ligand Bonds02:51

Metal-Ligand Bonds

25.7K
The hemoglobin in the blood, the chlorophyll in green plants, vitamin B-12, and the catalyst used in the manufacture of polyethylene all contain coordination compounds. Ions of the metals, especially the transition metals, are likely to form complexes.
In these complexes, transition metals form coordinate covalent bonds, a kind of Lewis acid-base interaction in which both of the electrons in the bond are contributed by a donor (Lewis base) to an electron acceptor (Lewis acid). The Lewis acid in...
25.7K
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

13.8K
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
13.8K

You might also read

Related Articles

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

Sort by
Same author

Self-assembly of a triple-zwitterion in polar solutions: hierarchical formation of nanostructures.

Soft matter·2026
Same author

Rational correction of pathogenic conformational defects in HTRA1.

Nature communications·2024
Same author

Distinctive Nucleic Acid Recognition by Lysine-Embedded Phenanthridine Peptides.

International journal of molecular sciences·2024
Same author

A Fluorophore-Labeled Lysine Dendrimer with an Oxo-Anion-Binding Motif for Tracking Gene Transfection.

Chembiochem : a European journal of chemical biology·2023
Same author

Impact of Peptide Sequences on Their Structure and Function: Mimicking of Virus-Like Nanoparticles for Nucleic Acid Delivery.

Chembiochem : a European journal of chemical biology·2022
Same author

Advances towards Cell-Specific Gene Transfection: A Small-Molecule Approach Allows Order-of-Magnitude Selectivity.

Chemistry (Weinheim an der Bergstrasse, Germany)·2022

Related Experiment Video

Updated: Apr 12, 2026

Author Spotlight: Improving the Production of Self-Assembling Fibers and Peptide Hydrogels for Superior Biocompatibility
05:24

Author Spotlight: Improving the Production of Self-Assembling Fibers and Peptide Hydrogels for Superior Biocompatibility

Published on: September 6, 2024

1.8K

Peptide self-assembly triggered by metal ions.

Rongfeng Zou1, Qi Wang, Junchen Wu

  • 1Key Lab for Advanced Materials and Institute of Fine Chemicals, East China University of Science and Technology, Shanghai 200237, China. tianhe@ecust.edu.cn jcwu@ecust.edu.cn.

Chemical Society Reviews
|May 9, 2015
PubMed
Summary

Chemists create artificial peptides that bind metal ions, mimicking natural proteins. This metal coordination drives peptide self-assembly for novel nanostructures and biotechnological applications.

More Related Videos

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

13.6K
A Tripeptide-Stabilized Nanoemulsion of Oleic Acid
10:42

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid

Published on: February 27, 2019

10.0K

Related Experiment Videos

Last Updated: Apr 12, 2026

Author Spotlight: Improving the Production of Self-Assembling Fibers and Peptide Hydrogels for Superior Biocompatibility
05:24

Author Spotlight: Improving the Production of Self-Assembling Fibers and Peptide Hydrogels for Superior Biocompatibility

Published on: September 6, 2024

1.8K
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

13.6K
A Tripeptide-Stabilized Nanoemulsion of Oleic Acid
10:42

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid

Published on: February 27, 2019

10.0K

Area of Science:

  • Biochemistry
  • Materials Science
  • Nanotechnology

Background:

  • Naturally occurring proteins utilize metal ions for biological functions.
  • Artificial peptides (coordination peptides) are designed to bind metal ions.
  • Understanding peptide-metal interactions is crucial for designing new coordination peptides.

Purpose of the Study:

  • To review strategies for metal-coordination-induced peptide self-assembly.
  • To describe the structures and functions of self-assembled peptide aggregates.
  • To highlight biotechnology applications of metal-induced peptide self-assembly.

Main Methods:

  • Review of existing literature on peptide self-assembly and metal coordination.
  • Analysis of natural and non-natural binding sites in peptides.
  • Examination of structural and functional properties of peptide-metal aggregates.

Main Results:

  • Metal coordination is a key strategy to control peptide self-assembly.
  • Diverse peptide aggregates with varied structures and functions can be formed.
  • Metal-induced peptide self-assembly shows promise for biotechnology.

Conclusions:

  • Metal coordination offers a powerful tool for designing self-assembling peptides.
  • Further research into peptide-metal interactions can unlock new biotechnological solutions.
  • This review provides insights into the field of metal-induced peptide self-assembly.