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Related Concept Videos

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...
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...
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...

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Monitoring Protein Adsorption with Solid-state Nanopores
08:51

Monitoring Protein Adsorption with Solid-state Nanopores

Published on: December 2, 2011

Protein adsorption in three dimensions.

Erwin A Vogler1

  • 1Department of Materials Science and Engineering, The Pennsylvania State University, University Park, PA 16802, USA. eav3@psu.edu

Biomaterials
|November 18, 2011
PubMed
Summary
This summary is machine-generated.

Understanding blood-protein adsorption to biomaterials is key for cardiovascular device development. This review clarifies protein adsorption kinetics and thermodynamics, proposing a new paradigm for surface science.

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Area of Science:

  • Biomaterials Surface Science
  • Physical Chemistry
  • Biophysical Chemistry

Background:

  • Blood-protein adsorption to biomaterials is a critical challenge in developing cardiovascular devices.
  • Inconsistencies in the protein adsorption literature stem from over five decades of research.
  • A fundamental understanding of protein adsorption is needed to address the 'protein-adsorption problem'.

Purpose of the Study:

  • To review and interpret experimental and theoretical work on blood-protein adsorption.
  • To provide a tutorial on the biophysical chemistry of protein adsorption.
  • To propose a revised paradigm for understanding protein adsorption to surfaces.

Main Methods:

  • Review and interpretation of existing literature on protein adsorption.
  • Discussion of protein adsorption kinetics and thermodynamics, including competitive adsorption.
  • Application of a three-dimensional interphase partitioning paradigm.

Main Results:

  • Protein adsorption can be rationalized by partitioning into a three-dimensional interphase.
  • Adsorbent hydrophilicity, surface energy, and protein concentration influence adsorption capacity.
  • Water's role in moderating protein adsorption via hydrogen bonding is significant.

Conclusions:

  • A unified paradigm explains protein adsorption kinetics and thermodynamics.
  • Adsorbent water wettability (surface energy) dictates protein adsorption capacity.
  • Proposed changes to the protein-adsorption paradigm may resolve key questions in biomaterials surface science.