 Inspired by molecular mechanisms that cells exploit to sense mechanical forces and convert them into biochemical signals, chemists dream of designing mechano-chemical switches integrated into materials. Using the adhesion protein fibronectin, where essentially each of its multiple repeats displays another molecular recognition motif, a computational model was derived asking how minimalistic designs of repeats translate into mechanical characteristics of their fibrillar assemblies: the hierarchy of repeat-unfolding within fibrils is not just controlled by their relative mechanical stabilities, as found for single molecules, but also by the strength of cryptic interactions between adjacent molecules that become activated by stretching. The forceinduced exposure of cryptic sites furthermore regulates the nonlinearity of stress-strain curves, the strain at which such fibers break, as well as the refolding kinetics and fraction of misfolded repeats. Gaining such computational insights at the mesoscale is significant since translating protein-based concepts into novel polymer designs has proven difficult. See also New and Notable
for LaTeX users @article{OPeleg2012-103,
author = {O. Peleg and T. Savin and G. V. Kolmakov and I. G. Salib and A. C. Balazs and M. Kr\"oger and V. Vogel},
title = {Fibers with integrated mechanochemical switches: Minimalistic design principles derived from fibronectin},
journal = {Biophys. J.},
volume = {103},
pages = {1909-1918},
year = {2012}
}
\bibitem{OPeleg2012-103} O. Peleg, T. Savin, G.V. Kolmakov, I.G. Salib, A.C. Balazs, M. Kr\"oger, V. Vogel,
Fibers with integrated mechanochemical switches: Minimalistic design principles derived from fibronectin,
Biophys. J. {\bf 103} (2012) 1909-1918.OPeleg2012-103
O. Peleg, T. Savin, G.V. Kolmakov, I.G. Salib, A.C. Balazs, M. Kr\"oger, V. Vogel
Fibers with integrated mechanochemical switches: Minimalistic design principles derived from fibronectin
Biophys. J.,103,2012,1909-1918 |
mk@mat.ethz.ch
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