Letter abstract
Nature Nanotechnology 3, 512 - 516 (2008)
Published online: 29 June 2008 | doi:10.1038/nnano.2008.168
Subject Categories: Molecular machines and motors | Nanobiotechnology | Nanomaterials | Nanosensors and other devices | Structural properties
Engineered elastomeric proteins with dual elasticity can be controlled by a molecular regulator
Abstract
Elastomeric proteins are molecular springs that confer excellent mechanical properties1, 2, 3, 4, 5 to many biological tissues and biomaterials. Depending on the role performed by the tissue or biomaterial, elastomeric proteins can behave as molecular springs1, 2, 6, 7 or shock absorbers3, 4, 5, 8, 9, 10. Here we combine single-molecule atomic force microscopy and protein engineering techniques to create elastomeric proteins that can switch between two distinct types of mechanical behaviour in response to the binding of a molecular regulator. The proteins are mechanically labile by design and behave as entropic springs with an elasticity that is governed by their configurational entropy. However, when a molecular regulator binds to the protein, it switches into a mechanically stable state and can act as a shock absorber. These engineered proteins effectively mimic and combine the two extreme forms of elastic behaviour found in natural elastomeric proteins, and thus represent a new type of smart nanomaterial that will find potential applications in nanomechanics and material sciences.
- Department of Chemistry, The University of British Columbia, Vancouver, British Columbia V6T 1Z1, Canada
Correspondence to: Hongbin Li1 e-mail: Hongbin@chem.ubc.ca
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