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 Organization

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....

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 Folding

Protein Folding

Signal Sequences and Sorting Receptors

Signal Sequences and Sorting Receptors

Signal sequences are short amino acid sequences that guide newly synthesized proteins to their proper location within the cell. Classical signal sequences are fifteen to sixty amino acids long and present at the N-terminus of a polypeptide chain. Each signal sequence has a conserved segment of basic residues towards their N terminus, a hydrophobic core, and a C-terminus rich in polar residues. The C-terminus also contains a signal cleavage site and features a -3 -1 sequence motif. The -3-1...

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...

You might also read

Related Articles

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

Sort by

Same author

Light and Dark Cycles Control the Structural Evolution of Photoresponsive Supramolecular Systems.

Angewandte Chemie (International ed. in English)·2026

Same author

Human-specific evolutionary genetic loss of addition of a single oxygen atom from sialic acids increases hydrophobicity of cells and proteins [Carbohydr. Res. (552), June 2025, 109469].

Carbohydrate research·2026

Same author

3D self-assembly of cyclic peptides into multilayered nanosheets.

Chemical science·2026

Same author

Emergent properties of supramolecular peptide assemblies.

Chemical communications (Cambridge, England)·2025

Same author

Arbuscular mycorrhizal association regulates global root-seed coordination.

Nature plants·2025

Same author

An aspirational approach to planetary futures.

Nature·2025

Same journal

Total Synthesis and Structural Revision of Tetracyclic Diterpenoid (±)-Papililone A and (-)-Papililone A.

Chemistry (Weinheim an der Bergstrasse, Germany)·2026

Same journal

Light-Powered Atroposelective Ratcheting via Excited-State Donor-Acceptor Interactions.

Chemistry (Weinheim an der Bergstrasse, Germany)·2026

Same journal

Modular One-Pot Access to π-Expanded Tetrakis(Phenothiazinyl)-Silanes With Broadly Tunable Redox and Emission Properties.

Chemistry (Weinheim an der Bergstrasse, Germany)·2026

Same journal

pH-Tolerant Tripeptide Coacervates as Biomimetic Catalytic Microreactors.

Chemistry (Weinheim an der Bergstrasse, Germany)·2026

Same journal

Nano-Nickel Pinned Defective MoS<sub>2</sub> Heterostructures via Ball Milling for Improved Hydrogen Evolution.

Chemistry (Weinheim an der Bergstrasse, Germany)·2026

Same journal

Hollow NiCo-LDH Nanocage Derived From ZIF-67 as an Efficient Catalyst for the Thermal Decomposition of Ammonium Perchlorate.

Chemistry (Weinheim an der Bergstrasse, Germany)·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Dec 11, 2025

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

Sequence Decoding of 1D to 2D Self-Assembling Cyclic Peptides.

Sandra Díaz¹, Ignacio Insua¹, Ghibom Bhak¹

¹Centro Singular de Investigación en Química Biolóxica e Materiais Moleculares (CIQUS), Departamento de Química Orgánica, Universidade de Santiago de Compostela, Santiago de Compostela, 15782, Spain.

Chemistry (Weinheim an Der Bergstrasse, Germany)

|August 26, 2020

Summary

This summary is machine-generated.

Researchers designed a novel peptide that self-assembles into one-dimensional nanotubes, which then form large two-dimensional (2D) nanosheets. This study maps the structure-assembly relationships crucial for creating advanced 2D peptide biomaterials.

Keywords:

2D nanosheet nanotube self-assembly supramolecular chemistry

More Related Videos

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Published on: February 6, 2020

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides

Published on: August 20, 2018

Related Experiment Videos

Last Updated: Dec 11, 2025

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

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Published on: February 6, 2020

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides

Published on: August 20, 2018

Area of Science:

Supramolecular chemistry
Materials science
Biomaterials engineering

Background:

Peptides' self-assembly properties enable synthetic biomaterial design.
Hierarchical assembly of peptides into complex dimensions is challenging.

Purpose of the Study:

To explore the structural basis of hierarchical self-assembly in a d/l-alternating cyclic octapeptide.
To identify key peptide sequence features for two-dimensional (2D) nanosheet formation.

Main Methods:

Synthesis and structural characterization of a d/l-alternating cyclic octapeptide.
Investigating self-assembly into one-dimensional (1D) nanotubes and subsequent 2D nanosheet formation.
Systematic amino acid mutations to map structure-assembly relationships.

Main Results:

The peptide self-assembled into 1D nanotubes that further organized into large 2D nanosheets (up to 500 μm long, 3.2 nm thick).
Nine peptide modifications were tested, revealing sequence features tolerated by the nanosheets.
Three variants showed compromised 2D assembly, highlighting critical structural determinants.

Conclusions:

Established structure-assembly relationships for 2D peptide nanosheet formation.
Provided insights for designing novel hierarchical peptide supramolecular biomaterials.
Demonstrated a pathway for creating large-scale 2D peptide materials through controlled self-assembly.