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Adsorption of Gases on Solids01:28

Adsorption of Gases on Solids

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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...
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Adsorption Isotherms I01:29

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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...
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Adsorption Isotherms II01:25

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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...
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Surfactants, named for their behavior at interfaces, positively adsorb at the interfaces of two phases, reducing interfacial tension. Their versatility as emulsifiers, detergents, and foaming agents stems from this ability. Surfactants, often termed amphiphiles, share the property of amphipathy, with molecules having both hydrophilic and hydrophobic portions. The hydrophilic part is called the head, and the hydrophobic part, including an elongated alkyl substituent, forms the tail.Surfactants...
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Monitoring Protein Adsorption with Solid-state Nanopores
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Protein adsorption, desorption, and aggregation mediated by solid-liquid interfaces.

Tatiana Perevozchikova1, Hirsh Nanda2, Douglas P Nesta3

  • 1Department of Chemical and Biomolecular Engineering, Center for Molecular and Engineering Thermodynamics, University of Delaware, Newark, Delaware 19716; Centerfor Neutron Research, National Institute of Standards and Technology, Gaithersburg, Maryland 20899.

Journal of Pharmaceutical Sciences
|April 8, 2015
PubMed
Summary
This summary is machine-generated.

Protein adsorption to silicon oxide interfaces can cause aggregation. This study investigated alpha-chymotrypsinogen (aCgn) and monoclonal antibody (IgG1) aggregation, finding that electrostatic interactions and protein unfolding influence particle formation.

Keywords:
adsorptiondesorptionneutron reflectivityparticle sizingprotein aggregationscatteringstability

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Area of Science:

  • Biophysical Chemistry
  • Materials Science
  • Protein Science

Background:

  • Protein adsorption at interfaces is a known cause of aggregation.
  • Understanding the mechanisms of protein aggregation is crucial for biopharmaceutical development.
  • Key stages of adsorption-mediated aggregation are challenging to study directly.

Purpose of the Study:

  • To characterize protein aggregation at water-silicon oxide interfaces.
  • To investigate the influence of pH and ionic strength on protein adsorption and aggregation.
  • To compare the interfacial behavior of alpha-chymotrypsinogen (aCgn) and a monoclonal antibody (IgG1).

Main Methods:

  • Utilized neutron reflectivity to study protein layers adsorbed to silicon oxide surfaces.
  • Employed a flow cell for in-situ analysis and rinse steps.
  • Characterized desorbed aggregates using neutron scattering, microscopy, and fluorescence spectroscopy.

Main Results:

  • IgG1 molecules adsorbed "flat" with minimal desorption, while aCgn showed resistance to desorption when unfolded.
  • Strong binding led to desorption of monomers and aggregates (aCgn) or subvisible particles (IgG1).
  • Electrostatic interactions significantly impacted protein adsorption and unfolding.

Conclusions:

  • Protein adsorption at SiOx interfaces can lead to aggregation, with distinct behaviors for aCgn and IgG1.
  • Unfolding and electrostatic interactions play critical roles in protein adsorption and subsequent aggregation.
  • The study provides insights into the mechanisms of protein aggregation relevant to biopharmaceutical stability.