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 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...

Assembly of Signaling Complexes

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...

Protein Folding

Protein Folding

Structure of Cadherins

Structure of Cadherins

The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins” is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This diversity of cadherins...

Mechanisms of Membrane Domain Formation

Mechanisms of Membrane Domain Formation

Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...

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.

You might also read

Related Articles

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

Sort by

Same author

Innovative peptide formulations for cardiovascular diseases using supercritical CO<sub>2</sub>: A comprehensive review and potential applications.

European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences·2026

Same author

Kinetics and Mechanism of the Enantioselective Passerini Multicomponent Reaction Catalyzed by Chiral Ionic Liquids.

ACS omega·2026

Same author

Unravelling the skin of the nurse shark: A morphological description of the placoid scales of Ginglymostoma cirratum.

Journal of fish biology·2026

Same author

More than a Thickener: Xanthan Gum as a Vehicle for the Herbicidal Extract of <i>Saussurea lappa</i> and Its Rheological Characterization.

Plants (Basel, Switzerland)·2026

Same author

A partially automated method for DNA extraction from marmoset hair follicles to avoid blood chimerism.

Frontiers in genetics·2025

Same author

Exploiting Spiropyran Solvatochromism for Heavy Metal Ion Detection in Aqueous Solutions.

ACS omega·2025

Search research articles

Related Experiment Video

Updated: May 25, 2026

Controlling the Size, Shape and Stability of Supramolecular Polymers in Water

Controlling the Size, Shape and Stability of Supramolecular Polymers in Water

Published on: August 2, 2012

Superstructure based on β-CD self-assembly induced by a small guest molecule.

Frederico B De Sousa¹, Ana C Lima, Angelo M L Denadai

¹Laboratório de Encapsulamento Molecular e Biomateriais (LEMB), Departamento de Química, Instituto de Ciências Exatas, Universidade Federal de Minas Gerais (UFMG), Belo Horizonte, 31270-901, MG, Brazil.

Physical Chemistry Chemical Physics : PCCP

|January 12, 2012

Summary

This summary is machine-generated.

This study determined the thermodynamic parameters and structure of beta-cyclodextrin (β-CD) self-assemblies for controlled drug release. Beta-cyclodextrin nanoparticle size and ampicillin complexation were characterized.

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

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

Related Experiment Videos

Last Updated: May 25, 2026

Controlling the Size, Shape and Stability of Supramolecular Polymers in Water

Controlling the Size, Shape and Stability of Supramolecular Polymers in Water

Published on: August 2, 2012

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

Area of Science:

Supramolecular Chemistry
Materials Science
Nanotechnology

Background:

Nanoparticle size, shape, and surface chemistry influence cellular interactions.
Controlled drug release systems require understanding self-assembly thermodynamics and structure.
Beta-cyclodextrin (β-CD) is a potential host molecule for drug encapsulation.

Purpose of the Study:

Determine β-CD self-assembly thermodynamic parameters and structure.
Investigate β-CD assemblies as a controlled drug release system.
Analyze the effect of ampicillin (AMP) on β-CD self-assembly.

Main Methods:

Light scattering measurements to determine critical aggregation concentration (cac) and thermodynamic parameters.
Debye's plot and molecular dynamic simulations for cluster analysis.
Nuclear magnetic resonance (NMR) and isothermal titration calorimetry (ITC) for supramolecular complexation studies.

Main Results:

Thermodynamic parameters for β-CD self-assembly: Δ(agg)G(o) = -16.31 kJ mol⁻¹, Δ(agg)H(o) = -26.48 kJ mol⁻¹, TΔ(agg)S(o) = -10.53 kJ mol⁻¹ at 298.15 K.
Nanoparticle sizes were 1.5 nm below cac and 60-120 nm above cac.
Ampicillin (AMP) did not affect β-CD's cac, and NMR/ITC identified different complex stoichiometries.

Conclusions:

β-CD self-assembly is thermodynamically favorable in aqueous solution.
The study provides insights into β-CD nanoparticle formation and drug complexation for controlled release applications.
Molecular dynamics and spectroscopic methods elucidated the supramolecular structure of β-CD:AMP systems.