Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Protein Organization

Protein Organization

Protein Folding

Protein Folding

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...

Protein Complex Assembly

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...

Protein and Protein Structure

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...

Peptide Bonds

Peptide Bonds

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...

You might also read

Related Articles

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

Sort by

Same author

ROS produced in mitochondria entrapped by self-assembly peptide fibers for target therapy of glioma.

Proceedings of the National Academy of Sciences of the United States of America·2026

Same author

Shape-Dependent Self-Assembled Targeting Peptide Electrosensitizer for Enhanced Radiofrequency Ablation of Lipid-Rich Atherosclerotic Plaques.

Journal of biomedical materials research. Part B, Applied biomaterials·2026

Same author

Living Inorganic Nanomaterials: Design, Preparation, and Biomedical Applications.

Advanced materials (Deerfield Beach, Fla.)·2026

Same author

Conformationally Variable Peptides Trap and Detoxify Ox-LDL in Plaques for Attenuating Atherosclerosis in Multiple Species.

Advanced materials (Deerfield Beach, Fla.)·2026

Same author

In situ self-assembled glycopeptide regulates tumor microenvironment for tumor immunotherapy.

Journal of controlled release : official journal of the Controlled Release Society·2026

Same author

Targeting and self-assembling peptides mimic fibrinogen coagulation for alleviating hypofibrinogenemia.

Biomaterials science·2026

Search research articles

Related Experiment Video

Updated: Jun 12, 2025

Author Spotlight: Optimization of Ultrashort Peptide Matrices for Colorectal Cancer Organoids

Author Spotlight: Optimization of Ultrashort Peptide Matrices for Colorectal Cancer Organoids

Published on: May 3, 2024

Self-Assembled Peptide with Morphological Structure for Bioapplication.

Yu Wang^1,2, Yusi Liao^2,3, Ying-Jin Zhang^1,2

¹Henan Institute of Advanced Technology, Zhengzhou University, Zhengzhou, 450052, P. R. China.

Biomacromolecules

|September 19, 2024

Summary

Self-assembled peptide biomaterials form diverse nanostructures like nanoparticles and nanofibers. This review explores their morphology, transformation mechanisms, and applications, envisioning future nanomaterial directions.

More Related Videos

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid

Published on: February 27, 2019

Related Experiment Videos

Last Updated: Jun 12, 2025

Author Spotlight: Optimization of Ultrashort Peptide Matrices for Colorectal Cancer Organoids

Author Spotlight: Optimization of Ultrashort Peptide Matrices for Colorectal Cancer Organoids

Published on: May 3, 2024

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid

Published on: February 27, 2019

Area of Science:

Biomaterials Science
Nanotechnology
Chemical Engineering

Background:

Peptide materials are crucial biomaterials with versatile applications.
Self-assembly driven by molecular interactions yields diverse macroscopic forms.
Research in self-assembled peptides has advanced from lab to clinical settings.

Purpose of the Study:

To review the various morphologies of self-assembled peptides.
To discuss the mechanisms and applications of morphology transformation.
To envision future directions for self-assembled nanomaterials.

Main Methods:

Literature review of self-assembled peptide research.
Analysis of different peptide morphologies (nanoparticles, nanovesicles, nanotubes, nanofibers).
Discussion of morphology transformation mechanisms and applications.

Main Results:

Self-assembled peptides form diverse nanostructures including nanoparticles, nanovesicles, nanotubes, and nanofibers.
Morphology transformation is influenced by interaction forces and can be controlled.
Significant progress has been made in translating laboratory findings to clinical applications.

Conclusions:

Self-assembled peptide nanomaterials offer a wide range of properties and functions.
Understanding morphology transformation is key to designing advanced peptide biomaterials.
Future research will likely focus on novel applications and improved control over self-assembly.