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

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...

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...

Amyloid Fibrils

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...

Cationic Chain-Growth Polymerization: Mechanism

Cationic Chain-Growth Polymerization: Mechanism

The cationic polymerization mechanism consists of three steps: initiation, propagation, and termination. In the initiation step of the polymerization process, the π bond of a monomer gets protonated by the Lewis acid catalyst, which is formed from boron trifluoride and water. The protonation of the π bond generates a carbocation stabilized by the electron‐donating group. In the propagation step, the π bond of the second monomer acts as a nucleophile and attacks the generated carbocation,...

Polymers

Polymers

The word polymer is derived from the Greek words “poly” which means “many” and “mer” which means “parts”. Polymers are long chains of molecules composed of repeating units of smaller molecules, known as monomers. They either occur naturally, such as DNA and proteins, or can be constructed synthetically, like plastics. They have varied structural characteristics, such as linear chains, branched chains, or complex networks, that contribute to the properties that they exhibit. Additionally,...

You might also read

Related Articles

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

Sort by

Same author

Headgroup-Dependent Thermotropic and Lyotropic Phase Behavior and Emulsifying Behavior of Guerbet Branched-Chain Glycolipids.

Langmuir : the ACS journal of surfaces and colloids·2026

Same author

Nanostructure and Collagen-Stimulating Activity of Cationic Pentapeptide Lipopeptides.

Journal of peptide science : an official publication of the European Peptide Society·2026

Same author

Potentials of Machine Learning in Predicting Key Features of Synthetic Antimicrobial Polymers.

ACS polymers Au·2026

Same author

Polyelectrolyte-like Behavior, pH-Dependent Self-Assembly, and Emulsion Stabilizing Properties of a Model Surfactant-like Peptide Bearing Pyridine Groups.

Biomacromolecules·2026

Same author

Lysine containing amphiphilic peptide-based non-cytotoxic soft materials with potential antifungal and antibacterial activities for 3D cell culture.

Soft matter·2026

Same author

Novel Palmitoyl Pentapeptides: Self-Assembly, Collagen Stimulation, Antioxidant Activity, and Influence of Skin Microbiota Health.

ACS omega·2026

Search research articles

Related Experiment Video

Updated: May 20, 2026

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

Published on: February 5, 2020

Altering peptide fibrillization by polymer conjugation.

Sabrina Dehn¹, Valeria Castelletto, Ian W Hamley

¹Key Centre for Polymers and Colloids, School of Chemistry, The University of Sydney, NSW, 2006, Australia.

Biomacromolecules

|July 10, 2012

Summary

Synthetic polymers can disrupt the self-assembly of amyloid peptides, enabling controlled formation of peptide-polymer nanomaterials. This strategy influences beta-sheet aggregation for targeted material design.

More Related Videos

Wet Chemistry and Peptide Immobilization on Polytetrafluoroethylene for Improved Cell-adhesion

Wet Chemistry and Peptide Immobilization on Polytetrafluoroethylene for Improved Cell-adhesion

Published on: August 15, 2016

Microwave-assisted Functionalization of Poly(ethylene glycol) and On-resin Peptides for Use in Chain Polymerizations and Hydrogel Formation

Microwave-assisted Functionalization of Poly(ethylene glycol) and On-resin Peptides for Use in Chain Polymerizations and Hydrogel Formation

Published on: October 29, 2013

Related Experiment Videos

Last Updated: May 20, 2026

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

Published on: February 5, 2020

Wet Chemistry and Peptide Immobilization on Polytetrafluoroethylene for Improved Cell-adhesion

Wet Chemistry and Peptide Immobilization on Polytetrafluoroethylene for Improved Cell-adhesion

Published on: August 15, 2016

Microwave-assisted Functionalization of Poly(ethylene glycol) and On-resin Peptides for Use in Chain Polymerizations and Hydrogel Formation

Microwave-assisted Functionalization of Poly(ethylene glycol) and On-resin Peptides for Use in Chain Polymerizations and Hydrogel Formation

Published on: October 29, 2013

Area of Science:

Biomaterials Science
Polymer Chemistry
Nanotechnology

Background:

Amyloid peptides, like beta-amyloid (Aβ), exhibit strong self-assembly into beta-sheet structures.
Controlling amyloid self-assembly is crucial for developing novel nanomaterials and understanding amyloid-related diseases.

Purpose of the Study:

To develop a strategy using synthetic polymers to modulate the self-assembly of amyloid peptides.
To investigate the impact of polymer conjugation on the aggregation behavior of modified Aβ(16-20) sequences.
To explore the potential for creating targeted, self-assembled polymeric nanomaterials.

Main Methods:

Solid-phase peptide synthesis (SPPS) for peptide preparation.
Reversible addition-fragmentation chain transfer (RAFT) polymerization for polymer synthesis.
Copper(I) catalyzed azide-alkyne cycloaddition (CuAAC) for peptide-polymer conjugation.
Characterization using infrared spectroscopy, Transmission Electron Microscopy (TEM), Circular Dichroism (CD), and Small-Angle X-ray Scattering (SAXS).

Main Results:

Successful synthesis of peptide-polymer conjugates using a convergent approach.
Demonstrated that attached polymers, specifically poly(N-isopropylacrylamide) and poly(hydroxyethylacrylate), partially disrupt the self-assembly of Aβ(16-20) peptides.
Evidence of altered aggregation patterns influenced by the beta-sheet forming abilities of the peptides.

Conclusions:

Synthetic polymers can effectively disturb the inherent self-assembly of amyloid peptides.
This approach offers a method to control and influence peptide aggregation.
Presents an innovative route for the targeted assembly of amyloid-like fibers into functional polymeric nanomaterials.