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

Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
Peptide Bonds02:43

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-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Intermolecular Forces03:13

Intermolecular Forces

Atoms and molecules interact through bonds (or forces): intramolecular and intermolecular. The forces are electrostatic as they arise from interactions (attractive or repulsive) between charged species (permanent, partial, or temporary charges) and exist with varying strengths between ions, polar, nonpolar, and neutral molecules. The different types of intermolecular forces are ion–dipole, dipole–dipole, hydrogen bonds, and dispersion; among these, dipole–dipole, hydrogen bonds, and dispersion...
Ligand Binding Sites02:40

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Van der Waals Interactions01:24

Van der Waals Interactions

Atoms and molecules interact with each other through intermolecular forces. These electrostatic forces arise from attractive or repulsive interactions between particles with permanent, partial, or temporary charges. The intermolecular forces between neutral atoms and molecules are ion–dipole, dipole–dipole, and dispersion forces, collectively known as van der Waals forces.

You might also read

Related Articles

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

Sort by
Same author

Multiplatform Benchtop NMR Interlaboratory Study of Model Liquid Dosage Forms of Pharmaceutical Products.

Analytical chemistry·2026
Same author

Impact of hydrodynamic, mechanical, and interfacial stress during downstream processing on adeno-associated virus serotype 8 and 9.

Journal of pharmaceutical sciences·2025
Same author

Quantifying Hydrogen Populations in Liquid Mixtures Using <sup>1</sup>H NMR Relaxometry.

Analytical chemistry·2025
Same author

Advancing Pharmaceutical Security: Noninvasive Detection of Falsified Vaccines and Drugs Using wNMR.

Pharmaceutical research·2025
Same author

<i>In-situ</i> biophysical characterization of high-concentration protein formulations using <i>w</i>NMR.

mAbs·2024
Same author

Correction: Preventive Pharmacovigilance: timely and precise prevention of adverse events through person-level patient screening and dose-level product surveillance.

Pharmaceutical research·2023

Related Experiment Video

Updated: May 12, 2026

Preparation of Mechanically Stable Self-Assembled Peptides Hydrogels
05:24

Preparation of Mechanically Stable Self-Assembled Peptides Hydrogels

Published on: September 6, 2024

An interplay between electrostatic and polar interactions in peptide hydrogels.

Katherine Joyner1, Marc B Taraban, Yue Feng

  • 1Department of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, Baltimore, MD, 21201.

Biopolymers
|April 26, 2013
PubMed
Summary

Chemical programmability in peptide hydrogels was explored by swapping glutamic acid for glutamine. The number of electrostatic interactions, not location, dictates hydrogel properties and fiber formation, enabling tailored biomaterial design.

More Related Videos

Microwave-assisted Functionalization of Poly(ethylene glycol) and On-resin Peptides for Use in Chain Polymerizations and Hydrogel Formation
15:33

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

Published on: October 29, 2013

Patterning Bioactive Proteins or Peptides on Hydrogel Using Photochemistry for Biological Applications
09:19

Patterning Bioactive Proteins or Peptides on Hydrogel Using Photochemistry for Biological Applications

Published on: September 15, 2017

Related Experiment Videos

Last Updated: May 12, 2026

Preparation of Mechanically Stable Self-Assembled Peptides Hydrogels
05:24

Preparation of Mechanically Stable Self-Assembled Peptides Hydrogels

Published on: September 6, 2024

Microwave-assisted Functionalization of Poly(ethylene glycol) and On-resin Peptides for Use in Chain Polymerizations and Hydrogel Formation
15:33

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

Published on: October 29, 2013

Patterning Bioactive Proteins or Peptides on Hydrogel Using Photochemistry for Biological Applications
09:19

Patterning Bioactive Proteins or Peptides on Hydrogel Using Photochemistry for Biological Applications

Published on: September 15, 2017

Area of Science:

  • Biomaterials Science
  • Supramolecular Chemistry
  • Chemical Engineering

Background:

  • Peptide-based hydrogels offer inherent chemical programmability for biomedical applications.
  • Natural amino acids provide diverse chemical moieties for material design.
  • Mixing-induced self-assembly of oppositely charged peptides forms hydrogels.

Purpose of the Study:

  • To investigate the impact of electrostatic versus polar interactions on peptide hydrogel properties.
  • To systematically study how amino acid substitution affects hydrogel mechanical characteristics and structure.
  • To guide the rational design of peptide-based biomaterials with specific properties.

Main Methods:

  • Forming peptide hydrogels via mixing-induced self-assembly of oppositely charged peptide modules.
  • Systematically replacing glutamic acid (E) with glutamine (Q) in a negatively charged peptide module.
  • Utilizing dynamic rheology to measure mechanical properties (elastic modulus G').
  • Employing small-angle X-ray scattering (SAXS) to analyze structural changes and fiber formation.
  • Measuring T2 relaxation times of H2O and trifluoroacetic acid to probe molecular dynamics.

Main Results:

  • The number of electrostatic interactions (E residues), not their location, determines the hydrogel's elastic modulus (G').
  • Increased electrostatic interactions accelerate peptide assembly and decrease T2 relaxation times.
  • Substitution from electrostatic (E) to polar (Q) interactions alters fibrous network formation, shifting from elongated fibers to no fiber assembly.
  • Hydrogel mechanical properties and self-assembly behavior are directly influenced by the balance of electrostatic and polar interactions.

Conclusions:

  • The study systematically reveals how incorporating electrostatic and polar interactions impacts peptide-based hydrogel systems.
  • The findings demonstrate that the quantity of electrostatic interactions is a key determinant of hydrogel mechanics and structure.
  • This research provides a framework for designing peptide-based biomaterials with precisely controlled properties for various applications.