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Related Concept Videos

Adsorption Isotherms I01:29

Adsorption Isotherms I

Adsorption isotherms are mathematical models that describe how molecules in a gas or liquid phase interact with surfaces. Two of the most common isotherm models are the Langmuir and Freundlich isotherms, which relate to Type I monolayer chemisorption. The Langmuir model is based on four key assumptions:• Adsorption cannot exceed monolayer coverage.• All surface sites are equivalent.• Molecules adsorb only at vacant sites.• There are no interactions between adsorbed molecules.Consider the...
Adsorption of Gases on Solids01:28

Adsorption of Gases on Solids

Adsorption is a process where molecules, known as the adsorbates, accumulate on a surface, which is referred to as the adsorbent or substrate. Occurring at the solid-gas interface, this phenomenon is crucial in various scientific and industrial contexts. The reverse of adsorption is desorption.Two types of adsorptions exist: physical (physisorption) and chemical (chemisorption). Physisorption involves gas molecules held to the solid's surface by relatively weak intermolecular van der Waals...
Adsorption Isotherms II01:25

Adsorption Isotherms II

Brunauer, Emmett, and Teller (BET) introduced a theory in 1938 that modified Langmuir's assumptions to explain multilayer physical adsorption. This theory is applicable to Type II isotherms and provides a more realistic picture of adsorption processes. The BET theory assumes a uniform solid surface with localized adsorption sites, where adsorption at one site doesn't affect adsorption at neighboring sites. This theory also allows for the possibility of additional molecules being adsorbed on top...
Analyte Adsorption and Distribution01:09

Analyte Adsorption and Distribution

In certain chromatographic separations, solutes transfer between the mobile phase and the stationary phase via sorption, which typically refers to the process of adsorption. For many chromatographic systems, the sorption process often depends on the polarity of the compounds—an expression of the overall dipole moment within the molecule. During the separation process, there is competition between the solute and solvent for adsorption to the stationary phase. Highly polar compounds and solvents...
Adhesion01:14

Adhesion

Adhesion occurs when one type of molecule is attracted to a different molecule. Water exhibits adhesive properties in the presence of polar surfaces, such as glass or cellulose in plants. For instance, when water is poured into a glass, the positively charged hydrogen molecules of water are more attracted to the negatively charged oxygen molecules in the silica than to the oxygen in neighboring water molecules.
Capillary action is a result of water’s adhesive tendencies. When a narrow glass...
Affinity Chromatography01:03

Affinity Chromatography

Affinity chromatography is a powerful technique extensively utilized for separating and purifying specific biomolecules from complex mixtures. It capitalizes on the highly selective binding between an analyte and its counterpart, such as antibody-antigen interactions. The counterpart is immobilized on the stationary phase, forming an affinity column. The stationary phase typically consists of solid support, such as agarose or porous glass beads, immobilizing the affinity ligand. The mobile...

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Updated: May 28, 2026

Monitoring Protein Adsorption with Solid-state Nanopores
08:51

Monitoring Protein Adsorption with Solid-state Nanopores

Published on: December 2, 2011

Protein adsorption characterization.

M Cristina L Martins1, Susana R Sousa, Joana C Antunes

  • 1Divisão de Biomateriais, INEB - Instituto de Engenharia Biomédica, Universidade do Porto, Porto, Portugal. cmartins@ineb.up.pt

Methods in Molecular Biology (Clifton, N.J.)
|November 2, 2011
PubMed
Summary
This summary is machine-generated.

Assessing adsorbed proteins on surfaces is challenging. This study details methods like radiolabeling, ellipsometry, and quartz crystal microbalance with dissipation (QCM-D) for analyzing protein adsorption on poly(ethylene terephthalate).

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Area of Science:

  • Biomaterials Science
  • Surface Chemistry
  • Biophysics

Background:

  • Protein adsorption at biological interfaces alters surface properties and protein structure.
  • Quantifying adsorbed proteins is difficult due to substrate association, unlike proteins in solution.
  • No single technique fully characterizes protein adsorption; a multi-technique approach is necessary.

Purpose of the Study:

  • To detail methodologies for measuring human serum albumin adsorption onto poly(ethylene terephthalate).
  • To present surface preparation techniques for specific analytical methods.
  • To highlight the need for multi-technique analysis in protein adsorption studies.

Main Methods:

  • Radiolabeling: For quantifying adsorbed protein mass.
  • Ellipsometry: For determining adsorbed protein layer thickness and refractive index.
  • Quartz Crystal Microbalance with Dissipation (QCM-D): For real-time monitoring of mass adsorption and viscoelastic properties.

Main Results:

  • Detailed protocols for applying radiolabeling, ellipsometry, and QCM-D to protein adsorption on poly(ethylene terephthalate).
  • Demonstration of how each technique provides complementary information on protein adsorption.
  • Insights into the preparation of polymeric surfaces for optimal analysis with each method.

Conclusions:

  • A multi-technique approach combining radiolabeling, ellipsometry, and QCM-D is essential for comprehensive characterization of protein adsorption.
  • Specific surface preparation is crucial for accurate measurements using different analytical techniques.
  • Understanding protein adsorption behavior is vital for applications in biomaterials and biological interfaces.