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Designed biomaterials to mimic the mechanical properties of muscles.

TitleDesigned biomaterials to mimic the mechanical properties of muscles.
Publication TypeJournal Article
Year of Publication2010
AuthorsLv, S, Dudek, DM, Cao, Y, Balamurali, MM, Gosline, J, Li, H
JournalNature (London, United Kingdom)
Pagination69 - 73
Date Published2010///
ISBN Number0028-0836
Keywordsbiomaterial artificial muscle elasticity resilin

The passive elasticity of muscle is largely governed by the I-band part of the giant muscle protein titin, a complex mol. spring composed of a series of individually folded Ig-like domains as well as largely unstructured unique sequences. These mech. elements have distinct mech. properties, and when combined, they provide the desired passive elastic properties of muscle, which are a unique combination of strength, extensibility and resilience. Single-mol. at. force microscopy (AFM) studies demonstrated that the macroscopic behavior of titin in intact myofibrils can be reconstituted by combining the mech. properties of these mech. elements measured at the single-mol. level. Here we report artificial elastomeric proteins that mimic the mol. architecture of titin through the combination of well-characterized protein domains GB1 and resilin. We show that these artificial elastomeric proteins can be photochem. crosslinked and cast into solid biomaterials. These biomaterials behave as rubber-like materials showing high resilience at low strain and as shock-absorber-like materials at high strain by effectively dissipating energy. These properties are comparable to the passive elastic properties of muscles within the physiol. range of sarcomere length and so these materials represent a new muscle-mimetic biomaterial. The mech. properties of these biomaterials can be fine-tuned by adjusting the compn. of the elastomeric proteins, providing the opportunity to develop biomaterials that are mimetic of different types of muscles. We anticipate that these biomaterials will find applications in tissue engineering as scaffold and matrix for artificial muscles. [on SciFinder(R)]