Engineered elastomeric proteins with dual elasticity can be controlled by a molecular regulator.
Elastomeric proteins are molecular springs that confer excellent mechanical properties to many biological tissues and biomaterials. Depending on the role performed by the tissue or biomaterial, elastomeric proteins can behave as molecular springs or shock absorbers. 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.
Cao
Yi
Y
Li
Hongbin
H
D004548:Elasticity; D020724:Elastomers / Q000737:chemistry*; D006801:Humans; D007141:Immunoglobulin Fc Fragments / Q000378:metabolism; D007074:Immunoglobulin G / Q000737:chemistry; D018625:Microscopy, Atomic Force; D049329:Nanostructures / Q000737:chemistry / Q000648:ultrastructure; D036103:Nanotechnology / Q000379:methods*; D009419:Nerve Tissue Proteins / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D011487:Protein Conformation; D011489:Protein Denaturation; D015202:Protein Engineering / Q000379:methods*; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D013291:Streptococcus / Q000737:chemistry; D013816:Thermodynamics
D020724:Elastomers; C029152:G-substrate; D007141:Immunoglobulin Fc Fragments; D007074:Immunoglobulin G; D009419:Nerve Tissue Proteins; D011506:Proteins