Hierarchical self-assembly of a coiled-coil peptide into fractal structure.
Here we report the hierarchical self-assembly of a cross-linkable coiled-coil peptide containing an internal cysteine. Atomic force microscopy (AFM) experiments revealed the fractal structure of the assemblies, and molecular simulations showed that the peptides cross-linked to form clusters of coiled-coils, which further assembled to form globules of tens of nanometers in diameter. Such hierarchical organization was modulated by pH or thiol-reducing agent. Exploitation of the fractal structures through chemical methods may be valuable for the fabrication of materials spanning multiple length scales.
Lomander
Andrea
A
Center for Biomedical Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139-4307, USA.
Hwang
Wonmuk
W
Zhang
Shuguang
S
D003198:Computer Simulation; D003460:Crystallization / Q000379:methods*; D003545:Cysteine / Q000032:analysis / Q000737:chemistry*; D017709:Fractals; D008422:Materials Testing; D008956:Models, Chemical; D008958:Models, Molecular; D046912:Multiprotein Complexes / Q000032:analysis / Q000737:chemistry / Q000648:ultrastructure; D049329:Nanostructures / Q000032:analysis / Q000737:chemistry* / Q000648:ultrastructure*; D010316:Particle Size; D010455:Peptides / Q000032:analysis / Q000737:chemistry*; D011487:Protein Conformation
D046912:Multiprotein Complexes; D010455:Peptides; D003545:Cysteine