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Controlling amphipathic peptide adsorption by smart switchable germanium interfaces.

Laura-Marleen Baumgartner1, Andreas Erbe1,2, Aimee L Boyle3

  • 1Department of Interface Chemistry and Surface Engineering, Max-Planck-Institut für Eisenforschung GmbH, Max-Planck-Str. 1, 40237 Düsseldorf, Germany. m.rabe@mpie.de.

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Summary

Researchers developed a smart germanium surface to control peptide adsorption. This breakthrough enables reversible biofouling prevention and advances bioanalytical tools and biosensors.

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Area of Science:

  • Surface chemistry
  • Biomaterials science
  • Electrochemistry

Background:

  • Controlling protein adsorption is crucial for preventing biofouling and enabling bioanalytical applications.
  • Existing methods often lack precise, reversible control over surface interactions.
  • Germanium (100) surfaces offer tunable properties through electrode potential manipulation.

Purpose of the Study:

  • To demonstrate *in situ* control of reversible peptide adsorption using an electrode potential-switchable germanium surface.
  • To investigate the influence of surface hydrophobicity and peptide charge on adsorption dynamics.
  • To explore the potential of this 'smart' interface for biofouling prevention and bioanalytical tools.

Main Methods:

  • Utilizing germanium (100) surface termination switching between hydrophobic (hydrogen-terminated) and hydrophilic (hydroxyl-terminated) states via electrode potential.
  • Employing polarized attenuated total reflection infrared (ATR-IR) spectroscopy to monitor peptide adsorption *in situ* at physiological pH in deuterated buffer.
  • Studying two model peptides with similar structures but opposite charges (amphipathic helices and coiled-coils) to differentiate hydrophobic and electrostatic interactions.

Main Results:

  • Demonstrated reversible adsorption and reorientation of peptides based on surface termination and peptide charge.
  • Achieved full control over negatively charged peptide adsorption by switching to the hydrophobic interface.
  • Observed a reversible tilting of the positively charged helical peptide upon switching to the hydrophobic surface.

Conclusions:

  • The developed 'smart' germanium interface enables precise, *in situ* control over peptide and protein adsorption.
  • This approach offers a versatile platform for biofouling prevention strategies.
  • The technology holds promise for developing advanced bioanalytical tools and functional biosensors.