Symmetric protein nanomaterials from novel co-assembling protein subunits

A run of protein-based materials papers (excluding yesterday’s dialysis paper).  Apologies for this – I do try to be diverse in content.  But this one is from my own journal Nature so I couldn’t resist.  Here it is.

Researchers have described the precise self-assembly of protein nanomaterials from two novel co-assembling protein subunits.  Computational methods were used to predict amino acid sequences (one for each subunit) which would stabilize the interfaces between the folded subunits and drive assembly of multiple copies into a specific symmetric architecture.  The researchers experimentally verified the computational methods by fabricating five different two-component co-asssembled nanomaterials each forming one of two targeted tetrahedral architectures.

Accurate design of co-assembling multi-component protein nanomaterials; N.P. King et al; Nature AOP; doi:10.1038/nature13404

http://www.nature.com/nature/journal/vaop/ncurrent/full/nature13404.html

Artificial biocomposites of silk fibroin and amyloid fibrils

Researchers have combined two widely-studied fibrous protein assemblies – silk fibroin fibrils and amyloid fibrils – into a novel composite material. By varying the weight ratio of the two components, mechanical properties could be tuned: more amyloid fibril increased tensile modulus whereas more silk fibroin promotes tougher composites. The amyloid component could be enzymatically removed to generate a porous silk membrane.  Inorganic components were also added and a shape memory effect observed.  

Modulating Materials by Orthogonally Oriented β-Strands: Composites of Amyloid and Silk Fibroin Fibrils; S. Ling et al; Advanced Materials; DOI: 10.1002/adma.201400730

http://onlinelibrary.wiley.com/doi/10.1002/adma.201400730/abstract