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Stability of tethered proteins.

Gaurav Anand1, Sumit Sharma, Sanat K Kumar

  • 1Howard P. Isermann Department of Chemical and Biological Engineering and Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York 12180-3590, USA.

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Summary

Tethered proteins like lysozyme (LYS) and ribonuclease A (RNase A) showed increased adhesion energy under denaturing conditions, indicating unfolding. However, they failed to refold, suggesting irreversible aggregation on the surface.

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Area of Science:

  • Protein stability studies
  • Surface science
  • Biophysics

Background:

  • Conventional protein structural methods are limited on solid substrates.
  • Tethered proteins present unique challenges for stability analysis.
  • Understanding protein behavior at interfaces is crucial for biomaterials and biosensors.

Purpose of the Study:

  • To investigate the stability of tethered globular proteins under denaturing conditions.
  • To explore protein unfolding and aggregation at surfaces.
  • To develop alternative methods for studying surface-bound proteins.

Main Methods:

  • Utilized multimolecular force spectroscopy with an atomic force microscope.
  • Employed functionalized hydrophobic (CH(3)-SAM) and carboxylic self-assembled monolayer (SAM) probes on gold-coated glass.
  • Monitored adhesion energy between the probe and tethered proteins (lysozyme and ribonuclease A).

Main Results:

  • Adhesion energy of tethered proteins peaked with increasing temperature or guanidinium hydrochloride (GuHCl) concentration.
  • Increased adhesion correlated with exposed hydrophobic protein cores.
  • Decreased adhesion at high denaturant levels indicated interprotein aggregation.
  • Tethered proteins did not recover their folded state upon cooling or GuHCl removal.
  • Diluting surface-tethered lysozyme reduced aggregation.

Conclusions:

  • Tethered proteins exhibit distinct unfolding and aggregation behaviors compared to solution-phase proteins.
  • Surface-induced aggregation appears to be irreversible under tested conditions.
  • Force spectroscopy provides a viable method for probing protein stability on solid surfaces.