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Open AccessJournal ArticleDOI

Self‐assembly of peptide amphiphiles: From molecules to nanostructures to biomaterials

Honggang Cui, +2 more
- 01 Jan 2010 - 
- Vol. 94, Iss: 1, pp 1-18
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TLDR
The strategies for using molecular self‐assembly as a toolbox to produce peptide amphiphile nanostructures and materials are highlighted and efforts to translate this technology into applications as therapeutics are reviewed.
Abstract
Peptide amphiphiles are a class of molecules that combine the structural features of amphiphilic surfactants with the functions of bioactive peptides and are known to assemble into a variety of nanostructures. A specific type of peptide amphiphiles are known to self-assemble into one-dimensional nanostructures under physiological conditions, predominantly nanofibers with a cylindrical geometry. The resultant nanostructures could be highly bioactive and are of great interest in many biomedical applications, including tissue engineering, regenerative medicine, and drug delivery. In this context, we highlight our strategies for using molecular self-assembly as a toolbox to produce peptide amphiphile nanostructures and materials and efforts to translate this technology into applications as therapeutics. We also review our recent progress in using these materials for treating spinal cord injury, inducing angiogenesis, and for hard tissue regeneration and replacement.

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Elucidating the Structure of Poly(dopamine)

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Peptide self-assembly: thermodynamics and kinetics

TL;DR: This review focuses on the influence of thermodynamic and kinetic factors on structural assembly and regulation based on different types of peptide building blocks, including aromatic dipeptides, amphiphilic peptides, polypeptide, and amyloid-relevant peptides.
References
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Journal ArticleDOI

Hybrid bone implants: self-assembly of peptide amphiphile nanofibers within porous titanium.

TL;DR: A method to prepare a hybrid bone implant material consisting of a Ti-6Al-4V foam, whose 52% porosity is filled with a peptide amphiphile (PA) nanofiber matrix, to improve fixation, osteointegration, and long term stability of implants is reported on.
Journal ArticleDOI

Supramolecular crafting of cell adhesion

TL;DR: Self-assembling supramolecular nanofibers that display the cell adhesion ligand RGDS at van der Waals density to cells are used and it is found that branched architectures of the monomers and the consequent lower packing efficiency and additional space for epitope motion improves signaling forcell adhesion, spreading, and migration.
Journal ArticleDOI

The carboxyl-terminal domain of phosphophoryn contains unique extended triplet amino acid repeat sequences forming ordered carboxyl-phosphate interaction ridges that may be essential in the biomineralization process

TL;DR: Two domains and the colocalization of Dmp1 and Dmp2 genes at a position equivalent to the dentinogenesis imperfecta type II location on human 4q21 all suggest that the PPs are indeed involved in some aspect of ECM mineralization.
Journal ArticleDOI

Molecular simulation study of peptide amphiphile self-assembly.

TL;DR: The results suggest that the formation of nanofibers of peptide amphiphiles obeys an open association model, which resembles living polymerization.
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