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Squaring the Circle in Peptide Assembly: From Fibers to Discrete Nanostructures by de Novo Design

Boyle, Aimee L.; Bromley, Elizabeth H. C.; Bartlett, Gail J.; Sessions, Richard B.; Sharp, Thomas H.; Williams, Claire L.; Curmi, Paul M. G.; Forde, Nancy R.; Linke, Heiner LU and Woolfson, Derek N. (2012) In Journal of the American Chemical Society 134(37). p.15457-15467
Abstract
The design of bioinspired nanostructures and materials of defined size and shape is challenging as it pushes our understanding of biomolecular assembly to its limits. In such endeavors, DNA is the current building block of choice because of its predictable and programmable self-assembly. The use of peptide- and protein-based systems, however, has potential advantages due to their more-varied chemistries, structures and functions, and the prospects for recombinant production through gene synthesis and expression. Here, we present the design and characterization of two complementary peptides programmed to form a parallel heterodimeric coiled coil, which we use as the building blocks for larger, supramolecular assemblies. To achieve the... (More)
The design of bioinspired nanostructures and materials of defined size and shape is challenging as it pushes our understanding of biomolecular assembly to its limits. In such endeavors, DNA is the current building block of choice because of its predictable and programmable self-assembly. The use of peptide- and protein-based systems, however, has potential advantages due to their more-varied chemistries, structures and functions, and the prospects for recombinant production through gene synthesis and expression. Here, we present the design and characterization of two complementary peptides programmed to form a parallel heterodimeric coiled coil, which we use as the building blocks for larger, supramolecular assemblies. To achieve the latter, the two peptides are joined via peptidic linkers of variable lengths to produce a range of assemblies, from flexible fibers of indefinite length, through large colloidal-scale assemblies, down to closed and discrete nanoscale objects of defined stoichiometry. We posit that the different modes of assembly reflect the interplay between steric constraints imposed by short linkers and the bulk of the helices, and entropic factors that favor the formation of many smaller objects as the linker length is increased. This approach, and the resulting linear and proteinogenic polypeptides, represents a new route for constructing complex peptide-based assemblies and biomaterials. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of the American Chemical Society
volume
134
issue
37
pages
15457 - 15467
publisher
The American Chemical Society
external identifiers
  • wos:000308830600054
  • scopus:84866495014
ISSN
1520-5126
DOI
10.1021/ja3053943
language
English
LU publication?
yes
id
715bfd43-9380-4fcf-a420-949bfda7c9cd (old id 3190171)
date added to LUP
2012-12-04 08:08:58
date last changed
2017-11-19 03:51:21
@article{715bfd43-9380-4fcf-a420-949bfda7c9cd,
  abstract     = {The design of bioinspired nanostructures and materials of defined size and shape is challenging as it pushes our understanding of biomolecular assembly to its limits. In such endeavors, DNA is the current building block of choice because of its predictable and programmable self-assembly. The use of peptide- and protein-based systems, however, has potential advantages due to their more-varied chemistries, structures and functions, and the prospects for recombinant production through gene synthesis and expression. Here, we present the design and characterization of two complementary peptides programmed to form a parallel heterodimeric coiled coil, which we use as the building blocks for larger, supramolecular assemblies. To achieve the latter, the two peptides are joined via peptidic linkers of variable lengths to produce a range of assemblies, from flexible fibers of indefinite length, through large colloidal-scale assemblies, down to closed and discrete nanoscale objects of defined stoichiometry. We posit that the different modes of assembly reflect the interplay between steric constraints imposed by short linkers and the bulk of the helices, and entropic factors that favor the formation of many smaller objects as the linker length is increased. This approach, and the resulting linear and proteinogenic polypeptides, represents a new route for constructing complex peptide-based assemblies and biomaterials.},
  author       = {Boyle, Aimee L. and Bromley, Elizabeth H. C. and Bartlett, Gail J. and Sessions, Richard B. and Sharp, Thomas H. and Williams, Claire L. and Curmi, Paul M. G. and Forde, Nancy R. and Linke, Heiner and Woolfson, Derek N.},
  issn         = {1520-5126},
  language     = {eng},
  number       = {37},
  pages        = {15457--15467},
  publisher    = {The American Chemical Society},
  series       = {Journal of the American Chemical Society},
  title        = {Squaring the Circle in Peptide Assembly: From Fibers to Discrete Nanostructures by de Novo Design},
  url          = {http://dx.doi.org/10.1021/ja3053943},
  volume       = {134},
  year         = {2012},
}