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Micromechanical Investigations on Films made of Recombinant Spider Silk Proteins and Silk Fibroin

Published online by Cambridge University Press:  01 February 2011

Frauke Junghans ,
Udo Conrad ,
Andreas Heilmann  and
Uwe Spohn
Frauke Junghans
Affiliation:
[email protected], Fraunhofer Institut for Mechanics of Materials, Biological Materials and Interfaces, Walter-Hülse-Strasse 1, Halle (Saale), N/A, Germany
Udo Conrad
Affiliation:
[email protected], Leibniz Institute, Institute of Plant Genetics and Crop Plant Research, Corrensstrasse 3, Gatersleben, N/A, Germany
Andreas Heilmann
Affiliation:
hei @wmh.fhg.de, Fraunhofer Institute for Mechanics of Materials, Biological Materials and Interfaces, Walter-Hülse-Strasse 1, Halle (Saale), N/A, Germany
Uwe Spohn
Affiliation:
[email protected], Fraunhofer Institute for Mechanics of Materials, Biological Materials and Interfaces, Walter-Hülse-Strasse 1, Halle (Saale), N/A, Germany
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Abstract

Films made of a recombinant spider silk protein and silk fibroin were prepared by spincoating and casting. Therefore the solubility of these substances was investigated in hexafluoroisopropa-nol, ionic liquids and concentrated salt solutions. The roughness and the thickness of the protein films were determined by the Atomic Force Microscopy (AFM) and by mechanical profilometry. The micromechanical behaviour was investigated by acoustic impedance analysis using a quartz crystal microbalance (QCMB) as well as by microindentation. Films with thickness less than 350 nm revealed an almost ideal elastic behaviour in the range of 5 to 75 MHz. At a higher film thickness the half-band-half width increases considerably and the films show a viscoelastic be-haviour with a considerable dissipation. The relative humidity significantly influences the me-chanical behaviour of protein films. Hence the micro-hardness and the ability of water adsorption were determined in dependence on the relative humidity.

Keywords

thin filmbiomaterialmicrostructure
Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 1062: Symposium NN – Protein and Peptide Engineering for Therapeutic and Functional Materials , 2007 , 1062-NN06-08
Copyright
Copyright © Materials Research Society 2008

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References

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