TY - JOUR
T1 - Recombinant Spidroins Fully Replicate Primary Mechanical Properties of Natural Spider Silk
AU - Bowen, Christopher H.
AU - Dai, Bin
AU - Sargent, Cameron J.
AU - Bai, Wenqin
AU - Ladiwala, Pranay
AU - Feng, Huibao
AU - Huang, Wenwen
AU - Kaplan, David L.
AU - Galazka, Jonathan M.
AU - Zhang, Fuzhong
N1 - Funding Information:
We thank Tavis Reed and Beryl Mpamo for their assistance with protein production and Srikanth Singamaneni, Sirimuvva Tadepalli, and Rohit Gupta for assistance with Raman microspectroscopy. We thank Randy Lewis and Xiaoxia Xia for helpful discussions. We thank Yanhe Ma, Peijian Zou, and Pengju Wang from the Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, for providing the synthetic DNA sequence of N. clavipes MaSp1. This work was supported by a Young Investigator Program from AFOSR (FA95501510174 to F.Z.) and an Early Career Faculty grant from NASA’s Space Technology Research Grants Program (NNX15AU45G to F.Z.). We also thank the NIH (P41EB002520) for support for this work.
Funding Information:
This work was supported by a Young Investigator Program from AFOSR (FA95501510174 to F.Z.) and an Early Career Faculty grant from NASA's Space Technology Research Grants Program (NNX15AU45G to F.Z.). We also thank the NIH (P41EB002520) for support for this work.
Publisher Copyright:
© 2018 American Chemical Society.
PY - 2018/9/10
Y1 - 2018/9/10
N2 - Despite significant efforts to engineer their heterologous production, recombinant spider silk proteins (spidroins) have yet to replicate the unparalleled combination of high strength and toughness exhibited by natural spider silks, preventing their use in numerous mechanically demanding applications. To overcome this long-standing challenge, we have developed a synthetic biology approach combining standardized DNA part assembly and split intein-mediated ligation to produce recombinant spidroins of previously unobtainable size (556 kDa), containing 192 repeat motifs of the Nephila clavipes dragline spidroin. Fibers spun from our synthetic spidroins are the first to fully replicate the mechanical performance of their natural counterparts by all common metrics, i.e., tensile strength (1.03 ± 0.11 GPa), modulus (13.7 ± 3.0 GPa), extensibility (18 ± 6%), and toughness (114 ± 51 MJ/m3). The developed process reveals a path to more dependable production of high-performance silks for mechanically demanding applications while also providing a platform to facilitate production of other high-performance natural materials.
AB - Despite significant efforts to engineer their heterologous production, recombinant spider silk proteins (spidroins) have yet to replicate the unparalleled combination of high strength and toughness exhibited by natural spider silks, preventing their use in numerous mechanically demanding applications. To overcome this long-standing challenge, we have developed a synthetic biology approach combining standardized DNA part assembly and split intein-mediated ligation to produce recombinant spidroins of previously unobtainable size (556 kDa), containing 192 repeat motifs of the Nephila clavipes dragline spidroin. Fibers spun from our synthetic spidroins are the first to fully replicate the mechanical performance of their natural counterparts by all common metrics, i.e., tensile strength (1.03 ± 0.11 GPa), modulus (13.7 ± 3.0 GPa), extensibility (18 ± 6%), and toughness (114 ± 51 MJ/m3). The developed process reveals a path to more dependable production of high-performance silks for mechanically demanding applications while also providing a platform to facilitate production of other high-performance natural materials.
UR - http://www.scopus.com/inward/record.url?scp=85052338217&partnerID=8YFLogxK
U2 - 10.1021/acs.biomac.8b00980
DO - 10.1021/acs.biomac.8b00980
M3 - Article
C2 - 30080972
AN - SCOPUS:85052338217
SN - 1525-7797
VL - 19
SP - 3853
EP - 3860
JO - Biomacromolecules
JF - Biomacromolecules
IS - 9
ER -