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

Structures of Solids02:22

Structures of Solids

Solids in which the atoms, ions, or molecules are arranged in a definite repeating pattern are known as crystalline solids. Metals and ionic compounds typically form ordered, crystalline solids. A crystalline solid has a precise melting temperature because each atom or molecule of the same type is held in place with the same forces or energy. Amorphous solids or non-crystalline solids (or, sometimes, glasses) which lack an ordered internal structure and are randomly arranged. Substances that...
Silica Gel Column Chromatography: Overview01:10

Silica Gel Column Chromatography: Overview

Silica gel column chromatography is a technique for separating compounds using a column packed with silica gel as the stationary phase. This method relies on differences in the polarity of compounds. Based on their polarities, compounds move between the stationary phase (silica gel) and the mobile phase (the solvent), forming discrete bands in the column.
Polar components tend to bind strongly to the silica gel, causing them to move slowly through the column. In contrast, nonpolar compounds...
SDS-PAGE01:27

SDS-PAGE

Gel electrophoresis is a method that separates biological macromolecules like nucleic acids or proteins by forcing them to pass through a gel matrix under an electric field.
A variation of gel electrophoresis, termed  polyacrylamide gel electrophoresis (PAGE), is commonly used for separating proteins according to their molecular size by passing them through a polyacrylamide gel. Because of the varying charges associated with amino acid side chains, PAGE can be used to separate intact proteins...
Ionic Crystal Structures02:42

Ionic Crystal Structures

Ionic crystals consist of two or more different kinds of ions that usually have different sizes. The packing of these ions into a crystal structure is more complex than the packing of metal atoms that are the same size.
Most monatomic ions behave as charged spheres, and their attraction for ions of opposite charge is the same in every direction. Consequently, stable structures for ionic compounds result (1) when ions of one charge are surrounded by as many ions as possible of the opposite...

You might also read

Related Articles

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

Sort by
Same author

ZIF-4 exhibiting high carbonic anhydrase-mimicking activities.

RSC advances·2026
Same author

Warming-induced methylmercury production undermines the effects of mercury mitigation in a temperate coastal bay.

Journal of hazardous materials·2026
Same author

PROTAC-Based Proteomics Strategy Uncovers Arsenic-Binding Proteomes.

Analytical chemistry·2026
Same author

Tetrathiafulvalene Shuttling Electrons between Copper-MOFs and Electrodes for Glucose Oxidation and Fuel Cells.

ACS applied materials & interfaces·2026
Same author

Understanding microbial mercury methylation via metabolic pathways: Processes associated with one-carbon metabolism.

Journal of hazardous materials·2026
Same author

Speciation analysis reveals intracellular distribution of arsenicals among subcellular organelles of arsenic-methylated human cells exposed to arsenite.

Talanta·2026

Related Experiment Video

Updated: May 20, 2026

Low Molecular Weight Protein Enrichment on Mesoporous Silica Thin Films for Biomarker Discovery
13:00

Low Molecular Weight Protein Enrichment on Mesoporous Silica Thin Films for Biomarker Discovery

Published on: April 17, 2012

Intramesoporous silica structure differentiating protein loading density.

Wen Qi1, Xiaolin Li, Baowei Chen

  • 1Pacific Northwest National Laboratory, P. O. Box 999, Richland, WA 99352, USA.

Materials Letters
|June 30, 2012
PubMed
Summary

Hydrothermal aging influences mesoporous silica structure, impacting protein loading. Pore size and surface area are key factors for loading neutral Immunoglobulin G and charged glucose oxidase, respectively.

More Related Videos

Surface Properties of Synthesized Nanoporous Carbon and Silica Matrices
09:31

Surface Properties of Synthesized Nanoporous Carbon and Silica Matrices

Published on: March 27, 2019

Preparation of Functional Silica Using a Bioinspired Method
08:04

Preparation of Functional Silica Using a Bioinspired Method

Published on: August 1, 2018

Related Experiment Videos

Last Updated: May 20, 2026

Low Molecular Weight Protein Enrichment on Mesoporous Silica Thin Films for Biomarker Discovery
13:00

Low Molecular Weight Protein Enrichment on Mesoporous Silica Thin Films for Biomarker Discovery

Published on: April 17, 2012

Surface Properties of Synthesized Nanoporous Carbon and Silica Matrices
09:31

Surface Properties of Synthesized Nanoporous Carbon and Silica Matrices

Published on: March 27, 2019

Preparation of Functional Silica Using a Bioinspired Method
08:04

Preparation of Functional Silica Using a Bioinspired Method

Published on: August 1, 2018

Area of Science:

  • Materials Science
  • Biotechnology
  • Nanotechnology

Background:

  • Mesoporous silica materials are widely used for protein adsorption and delivery.
  • Understanding the relationship between material structure and protein loading is crucial for optimizing applications.

Purpose of the Study:

  • To investigate the effect of hydrothermal aging temperature on the intramesoporous structure of mesoporous silica.
  • To determine how these structural changes influence the loading of different types of proteins.

Main Methods:

  • Mesoporous silica samples were prepared and subjected to hydrothermal aging at varying temperatures.
  • Protein loading experiments were conducted using neutral Immunoglobulin G (IgG) and charged glucose oxidase.
  • Fluorescence emission spectroscopy was used to analyze protein-ligand interactions within the mesopores.

Main Results:

  • Hydrothermal aging temperature critically affected the intramesoporous structure of mesoporous silica.
  • Larger desorption pore size enhanced loading for neutral Immunoglobulin G (IgG).
  • Increased surface area improved loading for charged glucose oxidase, which attached electrostatically in a monolayer.

Conclusions:

  • The intramesoporous structure of mesoporous silica significantly dictates protein loading capacity.
  • Protein loading is dependent on protein properties (charge, shape) and silica structural characteristics (pore size, surface area).
  • Neutral proteins like IgG may aggregate after monolayer formation, while charged proteins form monolayers via electrostatic interactions.