CUED Publications database

Fibers with integrated mechanochemical switches: minimalistic design principles derived from fibronectin.

Peleg, O and Savin, T and Kolmakov, GV and Salib, IG and Balazs, AC and Kröger, M and Vogel, V (2012) Fibers with integrated mechanochemical switches: minimalistic design principles derived from fibronectin. Biophys J, 103. pp. 1909-1918.

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Abstract

Inspired by molecular mechanisms that cells exploit to sense mechanical forces and convert them into biochemical signals, chemists dream of designing mechanochemical switches integrated into materials. Using the adhesion protein fibronectin, whose multiple repeats essentially display distinct molecular recognition motifs, we derived a computational model to explain how minimalistic designs of repeats translate into the mechanical characteristics of their fibrillar assemblies. The hierarchy of repeat-unfolding within fibrils is controlled not only 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 force-induced exposure of cryptic sites furthermore regulates the nonlinearity of stress-strain curves, the strain at which such fibers break, and the refolding kinetics and fraction of misfolded repeats. Gaining such computational insights at the mesoscale is important because translating protein-based concepts into novel polymer designs has proven difficult.

Item Type: Article
Uncontrolled Keywords: Amino Acid Motifs Amino Acid Sequence Biomechanical Phenomena Fibronectins Microfibrils Molecular Dynamics Simulation Molecular Sequence Data Polymers Protein Folding Repetitive Sequences, Amino Acid
Subjects: UNSPECIFIED
Divisions: Div C > Biomechanics
Depositing User: Cron Job
Date Deposited: 17 Jul 2017 19:11
Last Modified: 23 Nov 2017 04:11
DOI: