Built to be reversible
There has been some success in designing stable peptide filaments; however, mimicking the reversible assembly of many natural protein filaments is challenging. Dynamic filaments usually comprise independently folded and asymmetric proteins and using such building blocks requires the design of multiple intermonomer interfaces. Shen et al. report the design of self-assembling helical filaments based on previously designed stable repeat proteins. The filaments are micron scale, and their diameter can be tuned by varying the number of repeats in the monomer. Anchor and capping units, built from monomers that lack an interaction interface, can be used to control assembly and disassembly. — from Science
(A and B) Comparison of properties of our designed filaments
(blue) with those of native filaments (green). (A) The fraction of
total residue-residue interactions between (rather than within)
monomers. (B) Superhelical parameters. (C) Computational
design protocol.
Read the full report here: http://science.sciencemag.org/content/362/6415/705 (PDF)