β3-Tripeptides Coassemble into Fluorescent Hydrogels for Serial Monitoring in Vivo

Ketav Kulkarni, Juichien Hung, Alex J. Fulcher, Alex H.P. Chan, Andrew Hong, John S. Forsythe, Marie-Isabel Aguilar, Steven G. Wise, Mark P. Del Borgo

Research output: Contribution to journalLetterResearchpeer-review

3 Citations (Scopus)

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 languageEnglish
Pages (from-to)3843-3847
Number of pages5
JournalACS Biomaterials Science and Engineering
Volume4
Issue number11
DOIs
Publication statusPublished - 2 Oct 2018

Keywords

  • fluorescence
  • hydrogels
  • peptide biomaterials
  • self-assembly

Cite this

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title = "β3-Tripeptides Coassemble into Fluorescent Hydrogels for Serial Monitoring in Vivo",
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.",
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author = "Ketav Kulkarni and Juichien Hung and Fulcher, {Alex J.} and Chan, {Alex H.P.} and Andrew Hong and Forsythe, {John S.} and Marie-Isabel Aguilar and Wise, {Steven G.} and {Del Borgo}, {Mark P.}",
year = "2018",
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doi = "10.1021/acsbiomaterials.8b01065",
language = "English",
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pages = "3843--3847",
journal = "ACS Biomaterials Science and Engineering",
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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 journalLetterResearchpeer-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 -