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 Complex Assembly02:41

Protein Complex Assembly

12.6K
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...
12.6K

You might also read

Related Articles

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

Sort by
Same author

Combined MEK1/2 and Autophagy Inhibition Suppresses Tumor Growth via STING-Mediated Type I Interferon Response in iCCA.

Cancer science·2026
Same author

Retrospective analysis of adaptation frequencies and factors in offline in offline adaptive proton therapy.

Journal of applied clinical medical physics·2026
Same author

Radiogenomics deciphers tumor heterogeneity in hepatocellular carcinoma and combined hepatocellular-cholangiocarcinoma.

Discover oncology·2026
Same author

A postoperative recurrence prediction model for intrahepatic cholangiocarcinoma based on multi-omics analysis of adjacent-to-tumor tissues.

Frontiers in oncology·2026
Same author

Robust transcriptomic hallmarks targeting intratumor heterogeneity in intrahepatic cholangiocarcinoma.

Cell reports. Medicine·2026
Same author

Cavity acidification limits ferritin iron biomineralization.

Journal of inorganic biochemistry·2026

Related Experiment Video

Updated: May 6, 2026

Gold Nanoparticle Synthesis
13:42

Gold Nanoparticle Synthesis

Published on: July 10, 2021

14.9K

Engineering a well-ordered, functional protein-gold nanoparticle assembly.

Jasmina C Cheung-Lau1, Dage Liu, Katherine W Pulsipher

  • 1Department of Chemistry, University of Pennsylvania, 231 South 34th Street, Philadelphia, PA 19104-6323, United States.

Journal of Inorganic Biochemistry
|November 2, 2013
PubMed
Summary

Thermophilic ferritin (tF) efficiently encapsulates gold nanoparticles (AuNPs) under mild conditions. This protein-nanoparticle assembly is stable, reversible, and can template further gold nanoparticle growth.

Keywords:
BiomineralizationFerritin assemblyNanoparticle–protein interactionProtein self-assemblyProtein–nanoparticle association constant

More Related Videos

Author Spotlight: Direct Synthesis of EM-Visible Gold Nanoparticles in Cells for Protein Localization Analysis with Well-Preserved Ultrastructure
09:22

Author Spotlight: Direct Synthesis of EM-Visible Gold Nanoparticles in Cells for Protein Localization Analysis with Well-Preserved Ultrastructure

Published on: April 28, 2023

2.2K
A Technique to Functionalize and Self-assemble Macroscopic Nanoparticle-ligand Monolayer Films onto Template-free Substrates
08:09

A Technique to Functionalize and Self-assemble Macroscopic Nanoparticle-ligand Monolayer Films onto Template-free Substrates

Published on: May 9, 2014

10.4K

Related Experiment Videos

Last Updated: May 6, 2026

Gold Nanoparticle Synthesis
13:42

Gold Nanoparticle Synthesis

Published on: July 10, 2021

14.9K
Author Spotlight: Direct Synthesis of EM-Visible Gold Nanoparticles in Cells for Protein Localization Analysis with Well-Preserved Ultrastructure
09:22

Author Spotlight: Direct Synthesis of EM-Visible Gold Nanoparticles in Cells for Protein Localization Analysis with Well-Preserved Ultrastructure

Published on: April 28, 2023

2.2K
A Technique to Functionalize and Self-assemble Macroscopic Nanoparticle-ligand Monolayer Films onto Template-free Substrates
08:09

A Technique to Functionalize and Self-assemble Macroscopic Nanoparticle-ligand Monolayer Films onto Template-free Substrates

Published on: May 9, 2014

10.4K

Area of Science:

  • Biomaterials Science
  • Nanotechnology
  • Protein Engineering

Background:

  • Protein-nanoparticle interactions are crucial for advancing nanoparticle applications in biology, medicine, and materials science.
  • Ferritin, a protein cage, is explored for its potential in encapsulating nanoparticles.
  • Thermophilic ferritin (tF) offers enhanced stability, making it a candidate for nanoparticle encapsulation.

Purpose of the Study:

  • To investigate the encapsulation of gold nanoparticles (AuNPs) by thermophilic ferritin (tF).
  • To characterize the stability, assembly kinetics, and reversibility of the tF-AuNP complex.
  • To explore the templating capability of the tF-AuNP assembly for further nanoparticle synthesis.

Main Methods:

  • Encapsulation of 5-nm AuNPs by tF under mild conditions.
  • Chromatography-based assays to determine assembly time scales and reversibility.
  • Determination of apparent association constants (KA) using UV-Vis spectroscopy.
  • In-situ synthesis of larger AuNPs within the tF shell.

Main Results:

  • Nearly quantitative yield of 5-nm AuNP encapsulation by tF, preserving protein structure and activity.
  • Stable protein assembly around AuNPs occurred over ~48 hours and was found to be reversible.
  • High apparent association constants (KA) were determined for tF-AuNP complexes, comparable to salt-assembled ferritin.
  • The tF shell successfully templated the formation of 8-nm AuNPs with unchanged surface plasmon resonance.

Conclusions:

  • Thermophilic ferritin provides a stable and effective cage for encapsulating gold nanoparticles.
  • The tF-AuNP assembly exhibits reversible binding and can be utilized for templated nanoparticle synthesis.
  • This study highlights the potential of engineered ferritin proteins in nanomaterial fabrication and biomedical applications.