Centre current affairs

08/02/2010

The laboratory of José L. Toca-Herrera has published a full article about the recrystallization kinetics of bacterial proteins on substrates of different hydrophobicity, combining atomic force microscopy and quartz crystal microbalance with dissipation. The high resolution pictures showing crystal growth have been awarded with the frontispiece of the journal Small. This work is part of the PhD-Thesis of Aitziber Eleta López.

Article: "Surface Dependence of Protein Nanocrystal Formation"
Authors: A. Eleta López, S. Moreno-Flores, D. Pum, U. B. Sleytr and J. L. Toca-Herrera
Journal: Small, Volume 6, year: 2010, pages: 396-403


Bacterial S-layer proteins are able to self-assemble on many different surfaces to form nanostructured biomimetic crystals. We have studied this process on silicon dioxide and on silane-coated substrates. It has been found that substrate hydrophobicity affects protein adsorption rate and crystal domain size, but has no influence on the protein layer thickness, the crystal lattice parameters or the final adsorbed mass density. Analysis with a combination of atomic force microscopy and quartz crystal microbalance with dissipation monitoring showed that the S-protein crystal formation occurs in three steps: nucleation, growth (self-assembly) and domain reorganization.

 

This work has been supported by the Grant CTQ2007-66541 of the Spanish Ministry of Science and Innovation and the Department of Industry of the Basque Government (ETORTEK program)

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