Responsive gels formed by the spontaneous self-assembly of peptides into polymeric β-sheet tapes

@article{Aggeli1997ResponsiveGF,
  title={Responsive gels formed by the spontaneous self-assembly of peptides into polymeric $\beta$-sheet tapes},
  author={Amalia Aggeli and Mark Bell and N. Boden and Jeffery N. Keen and Peter F. Knowles and Tom C. B. McLeish and Maureen C. Pitkeathly and Sheena E. Radford},
  journal={Nature},
  year={1997},
  volume={386},
  pages={259-262}
}
Molecular self-assembly is becoming an increasingly popular route to new supramolecular structures and molecular materials1–7. The inspiration for such structures is commonly derived from self-assembling systems in biology. Here we show that a biological motif, the peptide β-sheet, can be exploited in designed oligopeptides that self-assemble into polymeric tapes and with potentially useful mechanical properties. We describe the construction of oligopeptides, rationally designed or based on… 
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689 Citations

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References

SHOWING 1-10 OF 31 REFERENCES
Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane.
TLDR
This work has shown that a 16-residue peptide has a characteristic beta-sheet circular dichroism spectrum in water and spontaneously assembles to form a macroscopic membrane, which may be a model for studying the insoluble peptides found in certain neurological disorders.
Chemical sequence control of beta-sheet assembly in macromolecular crystals of periodic polypeptides.
A family of uniform periodic polypeptides has been prepared by bacterial expression of the corresponding artificial genes, with the objective of exploring the potential for control of supramolecular…
Synthetic molecules that fold into a pleated secondary structure in solution
TLDR
The synthesis of molecules that will fold in water into a pleated structure is described, as a result of interactions between alternating electron-rich donor groups and electron-deficient acceptor groups.
Structural and mechanical properties of biopolymer gels
The structural and mechanical properties of gels formed from biopolymers are discussed both in terms of the techniques used to characterise these systems, and in terms of the systems themselves. The…
Nucleated Antiparallel β-Sheet That Folds and Undergoes Self-Assembly: A Template Promoted Folding Strategy toward Controlled Molecular Architectures
TLDR
The approach described here takes advantage of template driven hydrophobic clusters and template derived conformational biases to nucleate folding in small peptides, affording β-sheets which subsequently self-associate into fibrils.
Use of a gel‐forming dipeptide derivative as a carrier for antigen presentation
TLDR
Both the physical properties of the gel and its effect on the antigenicity of low molecular weight compounds suggest a number of practical applications.
A recipe for designing water‐soluble, β‐sheet‐forming peptides
TLDR
Results on four de novo designed, 33‐residue peptides are presented supporting the idea that under near physiologic conditions, all four peptide are soluble, form β‐sheet structures to varying degrees, and self‐associate.
Perspectives in Supramolecular Chemistry—From Molecular Recognition towards Molecular Information Processing and Self‐Organization
The selective binding of a substrate by a molecular receptor to form a supramolecular species involves molecular recognition which rests on the molecular information stored in the interacting…
Far-UV circular dichroism reveals a conformational switch in a peptide fragment from the beta-sheet of hen lysozyme.
TLDR
The conformation of a 20-residue synthetic peptide corresponding to the antiparallel triple-stranded beta-sheet in hen egg white lysozyme has been studied by circular dichroism (CD) and size-exclusion chromatography and it is found that the monomeric form of the peptide at low pH is predominantly random in nature.
Context-dependent secondary structure formation of a designed protein sequence
TLDR
The design of an 11-amino-acid sequence that folds as an α-helix when in one position but as a β-sheet when in another position of the primary sequence of the IgG-binding domain of protein G shows support for views of protein folding that favour tertiary interactions as dominant determinants of structure.
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