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Related Experiment Videos

Protein structural perturbation and aggregation on homogeneous surfaces.

Ananthakrishnan Sethuraman1, Georges Belfort

  • 1Department of Chemical and Biological Engineering, Rensselaer Polytechnic Institute, Troy, NY 12180, USA.

Biophysical Journal
|November 16, 2004
PubMed
Summary

Globular proteins lose structure and activity upon surface adsorption. Surface chemistry and protein concentration drive these conformational changes, impacting protein function.

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Area of Science:

  • Protein adsorption
  • Surface chemistry
  • Biophysics

Background:

  • Proteins undergo structural changes when interacting with surfaces.
  • Understanding these changes is crucial for biomaterial development and protein stability studies.

Purpose of the Study:

  • To investigate the structural stability and activity of hen egg lysozyme adsorbed on various solid surfaces.
  • To quantify secondary structure changes using spectroscopy and correlate them with protein activity.

Main Methods:

  • Attenuated total reflection/Fourier transformed infrared (ATR/FTIR) spectroscopy to monitor secondary structure.
  • Adsorption of lysozyme on self-assembled alkanethiol monolayers with diverse functional groups.
  • Activity assays to measure protein function post-adsorption.

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Main Results:

  • Lysozyme adsorbed on solid surfaces exhibited loss of native structure, transitioning from alpha-helix to turns/random and beta-sheet structures.
  • Increased intramolecular and intermolecular beta-sheet content indicated conformational rearrangement and aggregation.
  • Surface chemistry and adsorbate concentration significantly influenced structural perturbations and activity loss.

Conclusions:

  • Surface adsorption induces significant structural and functional changes in globular proteins like lysozyme.
  • ATR/FTIR spectroscopy is a valuable tool for in situ characterization of protein adsorption dynamics.
  • A kinetic model was proposed to describe the two-phase structural changes during protein adsorption.