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 Folding01:22

Protein Folding

119.8K
Overview
119.8K
Peptide Bonds02:43

Peptide Bonds

75.9K
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...
75.9K
Protein and Protein Structure02:15

Protein and Protein Structure

80.5K
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...
80.5K
Protein Organization01:13

Protein Organization

140.6K
Overview
140.6K
What are Proteins?01:28

What are Proteins?

15.1K
Proteins are polymers of amino acids linked together by peptide bonds. Proteins and polypeptides are interchangeably used to refer to long chains of amino acids. However, polypeptides have a molecular weight of fewer than 10,000 daltons, while proteins have greater molecular weight.  Polypeptides with less than 20 amino acids are called oligopeptides or simply peptides. Interactions among the constituent amino acid side chains of proteins help them fold into a stable 3-dimensional...
15.1K
Signal Sequences and Sorting Receptors01:41

Signal Sequences and Sorting Receptors

5.5K
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...
5.5K

You might also read

Related Articles

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

Sort by
Same author

Efficient Second-Harmonic Generation from Molecular Monolayers.

ACS nano·2026
Same author

Nonionic peptide amphiphiles and their supramolecular co-assemblies tune charge density and bioactivity.

Journal of materials chemistry. B·2026
Same author

Probing Supramolecular Motion with Nuclear Magnetic Resonance in Bioactive Scaffolds that Promote Neural Regeneration in the Central Nervous System.

Journal of the American Chemical Society·2026
Same author

Biodistribution and Biodegradation of an Osteoinductive Supramolecular Polymer Implant in a Rat Spinal Fusion Model.

Journal of functional biomaterials·2026
Same author

Design of Neuronal Supramolecular Scaffolds Integrating Cell Signaling and Electrical Conductivity.

ACS biomaterials science & engineering·2026
Same author

Prediction of rheological properties via structure elucidation of solvated hydrogels.

Nature materials·2026

Related Experiment Video

Updated: Aug 30, 2025

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid
10:42

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid

Published on: February 27, 2019

9.5K

Peptide Sequence Determines Structural Sensitivity to Supramolecular Polymerization Pathways and Bioactivity.

Shelby C Yuan1,2, Jacob A Lewis1,2, Hiroaki Sai2,3

  • 1Department of Biomedical Engineering, Northwestern University, Evanston, Illinois 60208, United States.

Journal of the American Chemical Society
|September 1, 2022
PubMed
Summary

Supramolecular polymer synthesis pathway impacts structure and function. AAEE monomers form ordered structures with weak cell interactions, while AEAE monomers yield less ordered, stronger hydrogels with enhanced cell adhesion.

More Related Videos

Synthesis and Mass Spectrometry Analysis of Oligo-peptoids
11:44

Synthesis and Mass Spectrometry Analysis of Oligo-peptoids

Published on: February 21, 2018

11.0K
Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
11:09

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Published on: August 1, 2018

10.8K

Related Experiment Videos

Last Updated: Aug 30, 2025

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid
10:42

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid

Published on: February 27, 2019

9.5K
Synthesis and Mass Spectrometry Analysis of Oligo-peptoids
11:44

Synthesis and Mass Spectrometry Analysis of Oligo-peptoids

Published on: February 21, 2018

11.0K
Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
11:09

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Published on: August 1, 2018

10.8K

Area of Science:

  • Supramolecular chemistry
  • Materials science
  • Biomaterials engineering

Background:

  • Supramolecular polymerization pathways influence material properties.
  • Peptide amphiphiles self-assemble into functional nanostructures.
  • Controlling supramolecular assembly is key for tailored material functions.

Purpose of the Study:

  • Investigate pathway-dependent supramolecular polymerization of isomeric peptide amphiphiles (AAEE and AEAE).
  • Determine how synthesis pathways affect internal nanostructure, hydrogel properties, and cell interactions.
  • Understand the role of dominant interactions in pathway sensitivity.

Main Methods:

  • Synthesized two isomeric peptide amphiphiles (AAEE, AEAE).
  • Applied five distinct polymerization pathways involving electrostatic screening and thermal annealing.
  • Characterized nanostructure, hydrogel porosity, mechanical strength, and cell-material interactions.

Main Results:

  • AAEE monomers formed crystalline structures with enhanced beta-sheet content under specific pathways (screening before annealing).
  • AEAE monomers showed less pathway dependence, forming less ordered structures with moderate beta-sheet content.
  • AEAE hydrogels exhibited lower porosity, higher mechanical strength, and promoted stronger cell interactions than AAEE hydrogels.

Conclusions:

  • Pathway sensitivity in supramolecular polymerization is dictated by dominant intermolecular interactions.
  • Tailoring synthesis pathways allows control over nanostructure, material properties, and biological function.
  • AEAE peptide amphiphiles offer a promising platform for biomaterials requiring robust mechanical properties and strong cell adhesion.