Issue 35, 2010

Effects of water on the structure and low/high temperature stability of confined proteins

Abstract

In this study well-characterized model proteins were confined in silica nanoporous matrices. Confinement of the proteins in silica matrices allowed us to explore the role of water hydrogen bonding on the structures of the proteins in a broad range of temperatures (−120 °C to 95 °C). At low temperatures confinement suppressed freezing of water, which remained in the liquid state. We obtained direct evidence that the changes in the hydrogen bonding of water induced changes in the structure of confined proteins. At high temperatures, a reduction of hydrogen bonding of water facilitated proteinsilica interactions and the confined proteins underwent denaturation. However, the incorporation of the osmolyte, trehalose, reduced proteinsilica interactions, and altered the hydrogen bonding of water. As a result, the high temperature thermal stability of the confined proteins was greatly improved.

Graphical abstract: Effects of water on the structure and low/high temperature stability of confined proteins

Supplementary files

Article information

Article type
Paper
Submitted
24 Feb 2010
Accepted
23 Jun 2010
First published
05 Aug 2010

Phys. Chem. Chem. Phys., 2010,12, 10161-10172

Effects of water on the structure and low/high temperature stability of confined proteins

E. Reátegui and A. Aksan, Phys. Chem. Chem. Phys., 2010, 12, 10161 DOI: 10.1039/C003517C

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