Abstract
β3-peptides uniquely form shear thinning hydrogels which are proteolytically stable and biocompatible. Herein we describe the synthesis, material and optical characterization of a new class of fluorescently labeled hydrogelators based on a helical N-acetylated β3-peptide backbone. The resulting hydrogels were analyzed using fluorescence microscopy to confirm successful incorporation of the fluorophore within the fiber matrix without compromising the β3-peptide self-assembly. Serial, noninvasive conscious animal imaging was used to monitor the injected hydrogel, delivered via subcutaneous injection, while tracking their degradation patterns in real-time. The hydrogels demonstrated persistent, high-intensity fluorescence when monitored over a 14-day period.
Original language | English |
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Pages (from-to) | 3843-3847 |
Number of pages | 5 |
Journal | ACS Biomaterials Science & Engineering |
Volume | 4 |
Issue number | 11 |
DOIs | |
Publication status | Published - 2 Oct 2018 |
Keywords
- fluorescence
- hydrogels
- peptide biomaterials
- self-assembly