Hierarchical self-assembly of a coiled-coil peptide into fractal structure. Academic Article

abstract

• 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.

authors

• Hwang, Wonmuk

published proceedings

• Nano Lett

author list (cited authors)

• Lomander, A., Hwang, W., & Zhang, S.

citation count

• 87

complete list of authors

• Lomander, Andrea||Hwang, Wonmuk||Zhang, Shuguang

publication date

• July 2005

publisher

• American Chemical Society (ACS)  Publisher

published in

• Nano Letters: a journal dedicated to nanoscience and nanotechnology  Journal

keywords

• Computer Simulation
• Crystallization
• Cysteine
• Fractals
• Materials Testing
• Models, Chemical
• Models, Molecular
• Multiprotein Complexes
• Nanostructures
• Particle Size
• Peptides
• Protein Conformation

PubMed Central ID

• 16178220

Digital Object Identifier (DOI)

• 10.1021/nl050203r

start page

• 1255

end page

• 1260

volume

• 5

issue

• 7

URL

• http://dx.doi.org/10.1021/nl050203r