Designed biomaterials to mimic the mechanical properties of muscles.
The passive elasticity of muscle is largely governed by the I-band part of the giant muscle protein titin, a complex molecular spring composed of a series of individually folded immunoglobulin-like domains as well as largely unstructured unique sequences. These mechanical elements have distinct mechanical properties, and when combined, they provide the desired passive elastic properties of muscle, which are a unique combination of strength, extensibility and resilience. Single-molecule atomic force microscopy (AFM) studies demonstrated that the macroscopic behaviour of titin in intact myofibrils can be reconstituted by combining the mechanical properties of these mechanical elements measured at the single-molecule level. Here we report artificial elastomeric proteins that mimic the molecular architecture of titin through the combination of well-characterized protein domains GB1 and resilin. We show that these artificial elastomeric proteins can be photochemically 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 physiological range of sarcomere length and so these materials represent a new muscle-mimetic biomaterial. The mechanical properties of these biomaterials can be fine-tuned by adjusting the composition 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.
Lv
Shanshan
S
Department of Chemistry, University of British Columbia, Vancouver, British Columbia V6T 1Z1, Canada.
Dudek
Daniel M
DM
Cao
Yi
Y
Balamurali
M M
MM
Gosline
John
J
Li
Hongbin
H
D000818:Animals; D001672:Biocompatible Materials / Q000138:chemical synthesis / Q000737:chemistry*; D001696:Biomechanical Phenomena; D032701:Biomimetics / Q000379:methods; D001704:Biopolymers / Q000737:chemistry*; D064211:Connectin; D004331:Drosophila melanogaster / Q000235:genetics; D004548:Elasticity; D009124:Muscle Proteins / Q000737:chemistry*; D020815:Polyproteins / Q000737:chemistry; D011494:Protein Kinases / Q000737:chemistry*; D013314:Stress, Mechanical
D001672:Biocompatible Materials; D001704:Biopolymers; D064211:Connectin; D009124:Muscle Proteins; D020815:Polyproteins; D011494:Protein Kinases
Biophys J. 2008 Oct;95(7):3358-65
18586853
Adv Biophys. 1996;33:159-71
8922111
Biochim Biophys Acta. 1964 Oct 9;93:213-5
14249161
J Cell Biol. 1999 Aug 9;146(3):631-44
10444071
Proc Natl Acad Sci U S A. 2001 Sep 11;98(19):10682-6
11526214
Nat Mater. 2007 Feb;6(2):109-14
17237787
FASEB J. 1997 Apr;11(5):341-5
9141500
Biopolymers. 2003 Dec;70(4):445-55
14648756
Nature. 2002 Aug 29;418(6901):998-1002
12198551
Connect Tissue Res. 1994;31(1):23-35
15609619
Nature. 2004 Apr 1;428(6982):487-92
15057821
Science. 1997 May 16;276(5315):1109-12
9148804
Science. 1995 Oct 13;270(5234):293-6
7569978
Biophys J. 2001 Mar;80(3):1442-51
11222304
J Biol Chem. 2002 Mar 29;277(13):11549-58
11799131
Biophys J. 1995 Mar;68(3):1027-44
7756523
Philos Trans R Soc Lond B Biol Sci. 2002 Feb 28;357(1418):169-84
11911774
Nature. 2005 Oct 13;437(7061):999-1002
16222249
Nature. 1997 May 15;387(6630):308-12
9153398
Eur J Biochem. 1997 Nov 15;250(1):92-8
9431995
Science. 1997 May 16;276(5315):1112-6
9148805
Nat Rev Mol Cell Biol. 2003 Sep;4(9):679-89
14506471
Adv Biophys. 1996;33:123-34
8922107
Philos Trans R Soc Lond B Biol Sci. 2002 Feb 28;357(1418):121-32
11911769
Circ Res. 1999 Jun 11;84(11):1339-52
10364572
Biomacromolecules. 2000 Spring;1(1):23-30
11709838
Macromol Biosci. 2005 Jun 24;5(6):502-11
15948227
Biophys J. 1994 Aug;67(2):782-92
7948691
Proc Natl Acad Sci U S A. 1999 Mar 30;96(7):3694-9
10097099
Proc Natl Acad Sci U S A. 1999 May 25;96(11):6020-4
10339534