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Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...

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Monitoring Protein Adsorption with Solid-state Nanopores
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Published on: December 2, 2011

Ordering surfaces on the nanoscale: implications for protein adsorption.

Andrew Hung1, Steve Mwenifumbo, Morgan Mager

  • 1Department of Materials, and Institute for Biomedical Engineering, Imperial College London , London, UK, SW7 2AZ.

Journal of the American Chemical Society
|January 7, 2011
PubMed
Summary

Monolayer-protected metal nanoparticles (MPMNs) show tunable protein adsorption based on ligand composition. Lysine residues are key to cytochrome C binding on these patterned nanomaterial surfaces.

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Area of Science:

  • Nanomaterials Science
  • Biomaterials Engineering
  • Protein-Surface Interactions

Background:

  • Monolayer-protected metal nanoparticles (MPMNs) possess tunable striped domain structures.
  • Nanostructuring influences biomolecule adsorption, critical for biomaterials design.

Purpose of the Study:

  • Investigate cytochrome C (Cyt C) interaction with MPMN surfaces.
  • Understand the role of surface chemistry and protein structure in adsorption.

Main Methods:

  • Experimental protein assays.
  • Computational molecular dynamics simulations (coarse-grained and atomistic).

Main Results:

  • Cyt C adsorption increases with MPMN surface polarity (hydrophilic interactions).
  • Adsorption enthalpy increases monotonically with surface polarity.
  • Lysine residues significantly facilitate Cyt C adsorption via dual-affinity interactions.

Conclusions:

  • Cyt C does not significantly disrupt its structure upon adsorption to MPMNs.
  • Lysine's amphipathic nature is crucial for binding to patterned nanomaterial surfaces.
  • Protein engineering with unnatural amino acids could enhance specific nanomaterial interactions.