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Polyprotein of GB1 is an ideal artificial elastomeric protein

Nature Materials volume 6, pages 109–114 (2007)Cite this article

Abstract

Naturally occurring elastomeric proteins function as molecular springs in their biological settings and show mechanical properties that underlie the elasticity of natural adhesives1, cell adhesion proteins2 and muscle proteins3. Constantly subject to repeated stretching–relaxation cycles, many elastomeric proteins demonstrate remarkable consistency and reliability in their mechanical performance3,4. Such properties had hitherto been observed only in naturally evolved elastomeric proteins. Here we use single-molecule atomic force microscopy techniques to demonstrate that an artificial polyprotein made of tandem repeats of non-mechanical protein GB1 has mechanical properties that are comparable or superior to those of known elastomeric proteins. In addition to its mechanical stability5, we show that GB1 polyprotein shows a unique combination of mechanical features, including the fastest folding kinetics measured so far for a tethered protein, high folding fidelity, low mechanical fatigue during repeated stretching–relaxation cycles and ability to fold against residual forces. These fine features make GB1 polyprotein an ideal artificial protein-based molecular spring that could function in a challenging working environment requiring repeated stretching–relaxation. This study represents a key step towards engineering artificial molecular springs with tailored nanomechanical properties for bottom-up construction of new devices and materials6.

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Figure 1: Polyprotein (GB1)8 has significant mechanical stability.
Figure 2: The fast folding kinetics of GB1.
Figure 3: GB1 can fold in the presence of residual forces.
Figure 4: Polyprotein (GB1)8 does not show noticeable mechanical fatigue.

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Acknowledgements

This work was supported by the Natural Sciences and Engineering Research Council of Canada, the Canada Research Chairs programme and the start-up fund from the University of British Columbia. Y.C. is partially supported by the Laird Fellowship.

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  1. Department of Chemistry, The University of British Columbia, Vancouver, BC, V6T 1Z1, Canada

    Yi Cao & Hongbin Li

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  1. Yi Cao
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Correspondence to Hongbin Li.

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Supplementary Information; Figures S1 and S2 (PDF 183 kb)

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Cao, Y., Li, H. Polyprotein of GB1 is an ideal artificial elastomeric protein. Nature Mater 6, 109–114 (2007). https://doi.org/10.1038/nmat1825

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