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 |
|---|---|
| Pages (from-to) | 3843-3847 |
| Number of pages | 5 |
| Journal | ACS Biomaterials Science and Engineering |
| Volume | 4 |
| Issue number | 11 |
| DOIs | |
| Publication status | Published - 2 Oct 2018 |
Keywords
- fluorescence
- hydrogels
- peptide biomaterials
- self-assembly
Cite this
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β3-Tripeptides Coassemble into Fluorescent Hydrogels for Serial Monitoring in Vivo. / Kulkarni, Ketav ; Hung, Juichien; Fulcher, Alex J.; Chan, Alex H.P.; Hong, Andrew; Forsythe, John S.; Aguilar, Marie-Isabel; Wise, Steven G.; Del Borgo, Mark P.
In: ACS Biomaterials Science and Engineering, Vol. 4, No. 11, 02.10.2018, p. 3843-3847.Research output: Contribution to journal › Letter › Research › peer-review
TY - JOUR
T1 - β3-Tripeptides Coassemble into Fluorescent Hydrogels for Serial Monitoring in Vivo
AU - Kulkarni, Ketav
AU - Hung, Juichien
AU - Fulcher, Alex J.
AU - Chan, Alex H.P.
AU - Hong, Andrew
AU - Forsythe, John S.
AU - Aguilar, Marie-Isabel
AU - Wise, Steven G.
AU - Del Borgo, Mark P.
PY - 2018/10/2
Y1 - 2018/10/2
N2 - 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.
AB - 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.
KW - fluorescence
KW - hydrogels
KW - peptide biomaterials
KW - self-assembly
UR - http://www.scopus.com/inward/record.url?scp=85054642421&partnerID=8YFLogxK
U2 - 10.1021/acsbiomaterials.8b01065
DO - 10.1021/acsbiomaterials.8b01065
M3 - Letter
VL - 4
SP - 3843
EP - 3847
JO - ACS Biomaterials Science and Engineering
JF - ACS Biomaterials Science and Engineering
SN - 2373-9878
IS - 11
ER -