Electric Field Directed Structural Modulation and Nanoassembly of Peptide Hydrogels.
The authors demonstrate that external electric fields can noninvasively alter the nanoscale supramolecular assembly, solubility, mechanical properties, and conductivity of designed short tripeptide hydrogels without changing peptide secondary structure.
What the AI sees
The authors demonstrate that external electric fields can noninvasively alter the nanoscale supramolecular assembly, solubility, mechanical properties, and conductivity of designed short tripeptide hydrogels without changing peptide secondary structure.
Research significance
Modulating peptide aggregation with electric fields is an intriguing, nonchemical approach that could conceivably be applied to reduce amyloid-like fibrillation (e.g., alpha-synuclein) relevant to Parkinson's, but this study uses artificial short peptides and lacks disease‑relevant proteins,…
Source abstract
This study presents a novel approach to modulate peptide self-assembly, solubility, and functional properties by utilizing an electric field as an external stimulus. Three short, heterochiral tripeptides, P1, P2, and P3, were designed based on their ability to form hydrogels. We demonstrate that the structural and functional properties of peptide-based hydrogels can be modulated upon exposure to an electric field. Our findings indicate that the external electric field does not alter the secondary structure of the designed peptides, however, the electric field plays a significant role in regulating the supramolecular assembly at the nanoscale. Morphological studies using field emission-scanning electron microscopy (FE-SEM), field emission-transmission electron microscopy (FE-TEM), and atomic force microscopy (AFM) images indicate a pronounced transition from a nanofibrillar architecture in control experiments with no electric field to the formation of nanoflakes, vesicular structures, and globular aggregates upon exposure to varying electric fields. We further examined the effect of the electric field in modulating the electrical conductivity of the peptide hydrogel. Additionally, an inverse relationship was observed between the peptide solubility and the mechanical robustness of the hydrogel. These findings suggest that the electric field can noninvasively perturb and modulate the solubility and aggregation characteristics of peptides. This approach also suggests a promising option for developing therapeutic interventions that enhance the solubility and reduce the fibrillation for several disease conditions, such as Alzheimer's and Parkinson's.