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Related Experiment Video

Updated: May 11, 2026

In Situ Characterization of Hydrated Proteins in Water by SALVI and ToF-SIMS
09:48

In Situ Characterization of Hydrated Proteins in Water by SALVI and ToF-SIMS

Published on: February 15, 2016

Elucidating changes in interfacial water structure upon protein adsorption.

J Kim1, P S Cremer

  • 1Department of Chemistry, Texas A&M University, College Station, TX 77842-3012, USA.

Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry
|May 21, 2013
PubMed
Summary
This summary is machine-generated.

Sum-frequency generation (SFG) spectroscopy revealed that bovine serum albumin (BSA) adsorption onto silica surfaces disorders interfacial water. This occurs due to a reduced surface charge, affecting hydrogen bonding in the water molecules.

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Probing the Structure and Dynamics of Interfacial Water with Scanning Tunneling Microscopy and Spectroscopy
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Probing the Structure and Dynamics of Interfacial Water with Scanning Tunneling Microscopy and Spectroscopy

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Last Updated: May 11, 2026

In Situ Characterization of Hydrated Proteins in Water by SALVI and ToF-SIMS
09:48

In Situ Characterization of Hydrated Proteins in Water by SALVI and ToF-SIMS

Published on: February 15, 2016

Probing the Structure and Dynamics of Interfacial Water with Scanning Tunneling Microscopy and Spectroscopy
10:28

Probing the Structure and Dynamics of Interfacial Water with Scanning Tunneling Microscopy and Spectroscopy

Published on: May 27, 2018

Area of Science:

  • Surface Chemistry
  • Spectroscopy
  • Biophysics

Background:

  • Protein adsorption is crucial in biological and industrial applications.
  • Understanding interfacial water structure during adsorption is key.
  • Silica surfaces and bovine serum albumin (BSA) are common models.

Purpose of the Study:

  • To investigate the effect of bovine serum albumin (BSA) adsorption on interfacial water structure at a silica surface.
  • To utilize sum-frequency generation (SFG) spectroscopy to probe these changes.
  • To correlate changes in water structure with surface properties like ξ-potential.

Main Methods:

  • Sum-frequency generation (SFG) spectroscopy was employed.
  • Bovine serum albumin (BSA) was adsorbed onto a silica surface from solution at pH 8.0.
  • Interfacial water structure and surface ξ-potential were analyzed.

Main Results:

  • BSA adsorption led to attenuated SFG intensity, indicating less ordered interfacial water.
  • A reduction in surface ξ-potential was observed.
  • The SFG spectrum revealed changes in hydrogen bonding of water molecules, with both stronger (≈3200 cm(-1)) and weaker (3200 cm(-1)) bonds.

Conclusions:

  • Protein adsorption significantly alters interfacial water ordering.
  • The observed changes in water structure are linked to modifications in surface charge (ξ-potential).
  • SFG spectroscopy is a powerful tool for studying complex surface phenomena like protein adsorption.