Unknown

Dataset Information

0

Dopamine Self-Polymerization as a Simple and Powerful Tool to Modulate the Viscoelastic Mechanical Properties of Peptide-Based Gels.


ABSTRACT: Dopamine is a small versatile molecule used for various biotechnological and biomedical applications. This neurotransmitter, in addition to its biological role, can undergo oxidative self-polymerization to yield polydopamine, a robust universal coating material. Herein, we harness dopamine self-polymerization to modulate the viscoelastic mechanical properties of peptide-based gels, expanding their ever-growing application potential. By combining rapid peptide assembly with slower dopamine auto-polymerization, a double network gel is formed, where the fibrillar peptide gel network serves as a scaffold for polydopamine deposition, allowing polydopamine to interpenetrate the gel network as well as establishing crosslinks within the matrix. We have shown that triggering the assembly of a lysine-rich peptide gelator in the presence of dopamine can increase the mechanical rigidity of the resultant gel by a factor of 90 in some cases, while retaining the gel's shear thin-recovery behavior. We further investigate how factors such as polymerization time, dopamine concentration and peptide concentration alter the mechanical properties of the resultant gel. The hybrid peptide-dopamine gel systems were characterized using rheological measurements, circular dichroism spectroscopy and transmission electron microscopy. Overall, triggering peptide gelation in the presence of dopamine represents a simple yet powerful approach to modulate the viscoelastic mechanical properties of peptide-based gels.

SUBMITTER: Fichman G 

PROVIDER: S-EPMC7961423 | biostudies-literature |

REPOSITORIES: biostudies-literature

Similar Datasets

| S-EPMC4358652 | biostudies-literature
| S-EPMC5510091 | biostudies-literature
| S-EPMC2597740 | biostudies-literature
2021-03-22 | PXD013343 | Pride
| S-EPMC7586293 | biostudies-literature
| S-EPMC8402770 | biostudies-literature
2015-02-02 | PXD001677 | Pride
| S-EPMC4086434 | biostudies-literature
| S-EPMC5456567 | biostudies-literature
| S-EPMC3462241 | biostudies-literature