Self-Assembled Surfactant Cyclic Peptide Nanostructures as Stabilizing Agents.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 24187575.
- Also identified by DOI 10.1039/C3SM50764E and PMC identifier 3811951.
- No licence information is recorded for this record.
- Because redistribution is not established, this page shows the abstract only. Follow the links below for the full text.
Abstract
A number of cyclic peptides including [FR]<sub>4</sub>, [FK]<sub>4</sub>, [WR]<sub>4</sub>, [CR]<sub>4</sub>, [AK]<sub>4</sub>, and [WK]<sub>n</sub> (n = 3-5) containing L-amino acids were produced using solid-phase peptide synthesis. We hypothesized that an optimal balance of hydrophobicity and charge could generate self-assembled nanostructures in aqueous solution by intramolecular and/or intermolecular interactions. Among all the designed peptides, [WR]<sub>n</sub> (n = 3-5) generated self-assembled vesicle-like nanostructures at room temperature as shown by transmission electron microscopy (TEM), scanning electron microscopy (SEM), and/or dynamic light scattering (DLS). This class of peptides represents the first report of surfactant-like cyclic peptides that self-assemble into nanostructures. A plausible mechanistic insight into the self-assembly of [WR]<sub>5</sub> was obtained by molecular modeling studies. Modified [WR]<sub>5</sub> analogues, such as [W<sub>Me</sub>R]<sub>5</sub>, [WR<sub>(Me)2</sub>]<sub>5</sub>, [W<sub>Me</sub>R<sub>(Me)2</sub>]<sub>5</sub>, and [W<i>d</i>R]<sub>5</sub>, exhibited different morphologies to [WR]<sub>5</sub> as shown by TEM observations. [WR]<sub>5</sub> exhibited a significant stabilizing effect for generated silver nanoparticles and glyceraldehyde-3-phosphate dehydrogenase activity. These studies established a new class of surfactant-like cyclic peptides that self-assembled into nanostructures and could have potential applications for the stabilization of silver nanoparticles and protein biomolecules.