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Biophys. J. BioFAST: First Published November 12, 2004. doi:10.1529/biophysj.104.051797
© 2004 by the Biophysical Society.

A more recent version of this article appeared on February 1, 2005.
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Georges Belfort
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PROTEINS

Protein Structural Perturbation and Aggregation on Homogeneous Surfaces

Ananthakrishnan Sethuraman 1 and Georges Belfort 1*

1 Rensselaer Polytechnic Institute

* To whom correspondence should be addressed. E-mail: belfog{at}rpi.edu.

Submitted on August 23, 2004
Revised on September 15, 2004
Accepted on 5 November 2004


  Abstract
We have demonstrated that globular proteins, such as hen egg lysozyme in phosphate buffered saline at room temperature, lose native structural stability and activity when adsorbed onto well-defined homogeneous solid surfaces. This structural loss is evident by {alpha}-helix to turns/random during the first thirty minutes and followed by a slow {alpha}-helix to {beta}-sheet transition. Increase in intramolecular and intermolecular {beta}-sheet content suggests conformational rearrangement and aggregation between different protein molecules, respectively. Amide-I-band ATR/FTIR spectroscopy was used to quantify the secondary structure content of lysozyme adsorbed on six different self-assembled alkanethiol monolayer surfaces (SAMs) with -CH3, -OPh, -CF3, -CN, -OCH3, and -OH exposed functional end-groups. Activity measurements of adsorbed lysozyme were in good agreement with the structural perturbations. Both surface chemistry (type of functional groups, wettability) and adsorbate concentration (i.e. lateral interactions) are responsible for the observed structural changes during adsorption. A kinetic model is proposed to describe secondary structural changes that occur in two dynamic phases. The results presented in this paper demonstrate the utility of the ATR/FTIR spectroscopic technique for in-situ characterization of protein secondary structures during adsorption on flat surfaces.

Key Words: activity, aggregation, protein folding, protein-surface interactions, secondary structure




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Copyright © 2004 by the Biophysical Society.