Power struggles in peptide-amphiphile nanostructures
- 20 July 2010
- journal article
- review article
- Published by Royal Society of Chemistry (RSC) in Chemical Society Reviews
- Vol. 39 (9), 3434-3444
- https://doi.org/10.1039/b919446k
Abstract
Inspired by the ubiquitous functions fulfilled by native proteins, the self-assembly of peptide amphiphiles (PAs) holds much promise for the creation of functional nanostructures. Typically, PAs are constructed by conjugating blocks of very different character: a hydrophilic peptide segment with a hydrophobic element (an alkyl chain, lipid, polymer or polypeptide). The resulting amphiphilicity governs the self-assembly process in aqueous solutions. This self-assembly process is guided by attractive forces (for example hydrophobic interactions, hydrogen bonding, electrostatic attraction) and repulsive forces (for example electrostatic repulsion, mechanical forces). The balance between these forces is responsible for the secondary structure of the peptide segment, and furthermore the size and shape of the assemblies that are formed. A result of PA self-assembly is that the properties of the peptide segment can be altered, as it is a general observation that peptides are more likely to exhibit a well-defined secondary structure at an interface (e.g. the corona of a micelle) than they are in solution. This characteristic of peptides can be exploited to give nanostructures with well-defined properties. The art of controlled PA self-assembly consists of carefully combining all the inter- and intramolecular forces to arrive at a material which is both structurally well-defined and has controllable functionalities. In this tutorial review the forces that act within PA nanostructures are discussed, that is, the effect of the hydrophobic block and peptide secondary structure on each other as well as on the aggregate as a whole. At the end of the review, a short section is devoted to the applications of these PA nanostructures.Keywords
This publication has 47 references indexed in Scilit:
- Development of bioactive peptide amphiphiles for therapeutic cell deliveryActa Biomaterialia, 2010
- Wormlike Micelle Formation in Peptide-Lipid Conjugates Driven by Secondary Structure Transformation of the HeadgroupsThe Journal of Physical Chemistry B, 2009
- Mechanisms of Peptide Amphiphile Internalization by SJSA-1 Cells in VitroBiochemistry, 2009
- Self-Assembly of Giant Peptide NanobeltsNano Letters, 2009
- Oligo(p-phenylenevinylene)−Peptide Conjugates: Synthesis and Self-Assembly in Solution and at the Solid−Liquid InterfaceJournal of the American Chemical Society, 2008
- Noncovalent Triblock Copolymers Based on a Coiled-Coil Peptide MotifJournal of the American Chemical Society, 2008
- Self-Assembling Nanofibers Inhibit Glial Scar Formation and Promote Axon Elongation after Spinal Cord InjuryJournal of Neuroscience, 2008
- Self‐Organizing β‐Sheet Lipopeptide Monolayers as Template for the Mineralization of CaCO3Angewandte Chemie, 2006
- Membrane‐Mimetic Nanocarriers Formed by a Dipalmitoylated Cell‐Penetrating PeptideAngewandte Chemie, 2005
- PEG-Based Hybrid Block Copolymers Containing α-Helical Coiled Coil Peptide Sequences: Control of Self-Assembly and Preliminary Biological EvaluationMacromolecules, 2005