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G-Protein Gated Ion Channels

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GPCRs are primarily responsible for our sense of smell, taste, and vision.  The binding of a sensory stimulus activates GPCR to stimulate effector proteins, many of which are ion channels in the sensory organs. GPCRs modulate the opening and closing of the target ion channels either directly by binding them, or by releasing second messengers that activate these channels. As ions move across the membrane, the membrane potential is altered, which induces an appropriate response.
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Multivalent-Ion-Activated Protein Adsorption Reflecting Bulk Reentrant Behavior.

Madeleine R Fries1, Daniel Stopper2, Michal K Braun1

  • 1Institute for Applied Physics, University of Tübingen, 72076 Tübingen, Germany.

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|December 30, 2017
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Summary
This summary is machine-generated.

Controlling protein adsorption at interfaces is key for biological processes. Multivalent ions influence bovine serum albumin adsorption, revealing insights into protein interactions and interface behavior.

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Area of Science:

  • Physical Chemistry
  • Biophysics
  • Materials Science

Background:

  • Protein adsorption at solid-liquid interfaces is a crucial initial step in many biological processes.
  • Microscopic mechanisms governing protein adsorption remain incompletely understood.
  • Controlling protein adsorption is vital for applications in biosensing, drug delivery, and biomaterials.

Purpose of the Study:

  • To investigate the influence of multivalent ions on the adsorption of net-negatively charged proteins at a solid-liquid interface.
  • To elucidate the microscopic mechanisms controlling protein-interface interactions.
  • To connect bulk phase behavior with interfacial adsorption phenomena.

Main Methods:

  • Ellipsometry was used to measure protein adsorption.
  • Neutron reflectivity and quartz-crystal microbalance experiments corroborated the findings.
  • A model of ion-activated patchy interactions within classical density functional theory was employed.

Main Results:

  • Multivalent ions effectively controlled the adsorption of bovine serum albumin (a net-negatively charged protein).
  • Reentrant condensation in bulk phase behavior was mirrored in protein adsorption at the interface.
  • The observed adsorption behavior exhibited a nonmonotonic dependence on salt concentration.

Conclusions:

  • The study successfully demonstrates control over protein adsorption using multivalent ions.
  • Findings provide a mechanistic understanding of ion-protein-interface interactions.
  • The work has implications for understanding nucleation at interfaces and designing biomaterial interfaces.