Peptide hydrogels as slow-release formulations of protein therapeutics : case study of asparaginase-loaded hydrogels
- Author
- Hue Vu (UGent) , Evelien Peeters (UGent) , Kenneth Hofkens (UGent) , Katrien Vandemeulebroecke (UGent) , Sara T'Sas (UGent) , Charlotte Martin (UGent) , Steven Ballet (UGent) , Richard Hoogenboom (UGent) , Steven Goossens (UGent) , Tim Lammens (UGent) , Maaike Van Trimpont (UGent) and Annemieke Madder (UGent)
- Organization
- Project
-
- Towards clinical testing of improved, less toxic and less immunogenic, L-asparaginase preparations for the treatment of acute lymphoblastic leukemia
- An alternative more tolerable L-asparaginase variant for the treatment of metastatic breast cancer
- Towards clinical testing of improved, less toxic and less immunogenic, L-asparaginase formulations for the treatment of ovarian cancer
- Establishing safety and efficacy of an improved Asparaginase in dog models: final preparation for Phase I clinical trial
- Molecular engineering of peptide-based hydrogels for sustained drug release
- Abstract
- In this study, hexamer peptide-based hydrogels were loaded with different model protein cargos and the release profiles investigated to explore the balance between injectability and loading capacity permitting the release of a therapeutically relevant dose. We demonstrate that the release of protein cargos from our hexamer peptide hydrogels depends on the stability of the hydrogel network, the mobility of the cargo to diffuse out of the network, and the interaction between the hydrogel network and the cargo. For the first time, our peptide hydrogels were used to develop an injectable sustained release formulation of a thera- peutic enzyme, namely Erwinase®, an FDA-approved asparaginase for the treatment of acute lympho- blastic leukemia. We show that the current hexamer peptide-based hydrogels allow sufficient protein loading and sustained release of the fully active asparaginase enzyme both in vitro and in vivo. Altogether, this study describes how peptide hydrogels can be exploited to provide injectable slow-release formu- lations of biologics, including enzyme therapeutics, to enhance their clinical applicability.
- Keywords
- ERWINIA-CHRYSANTHEMI, DRUG-RELEASE, DELIVERY, DESIGN
Downloads
-
definitieve versie van publisher version.pdf
- full text (Published version)
- |
- open access
- |
- |
- 1.55 MB
Citation
Please use this url to cite or link to this publication: http://hdl.handle.net/1854/LU-01JYEEC70JBJC947PH4C5NPFN1
- MLA
- Vu, Hue, et al. “Peptide Hydrogels as Slow-Release Formulations of Protein Therapeutics : Case Study of Asparaginase-Loaded Hydrogels.” BIOMATERIALS SCIENCE, vol. 13, no. 15, 2025, pp. 4139–52, doi:10.1039/d5bm00138b.
- APA
- Vu, H., Peeters, E., Hofkens, K., Vandemeulebroecke, K., T’Sas, S., Martin, C., … Madder, A. (2025). Peptide hydrogels as slow-release formulations of protein therapeutics : case study of asparaginase-loaded hydrogels. BIOMATERIALS SCIENCE, 13(15), 4139–4152. https://doi.org/10.1039/d5bm00138b
- Chicago author-date
- Vu, Hue, Evelien Peeters, Kenneth Hofkens, Katrien Vandemeulebroecke, Sara T’Sas, Charlotte Martin, Steven Ballet, et al. 2025. “Peptide Hydrogels as Slow-Release Formulations of Protein Therapeutics : Case Study of Asparaginase-Loaded Hydrogels.” BIOMATERIALS SCIENCE 13 (15): 4139–52. https://doi.org/10.1039/d5bm00138b.
- Chicago author-date (all authors)
- Vu, Hue, Evelien Peeters, Kenneth Hofkens, Katrien Vandemeulebroecke, Sara T’Sas, Charlotte Martin, Steven Ballet, Richard Hoogenboom, Steven Goossens, Tim Lammens, Maaike Van Trimpont, and Annemieke Madder. 2025. “Peptide Hydrogels as Slow-Release Formulations of Protein Therapeutics : Case Study of Asparaginase-Loaded Hydrogels.” BIOMATERIALS SCIENCE 13 (15): 4139–4152. doi:10.1039/d5bm00138b.
- Vancouver
- 1.Vu H, Peeters E, Hofkens K, Vandemeulebroecke K, T’Sas S, Martin C, et al. Peptide hydrogels as slow-release formulations of protein therapeutics : case study of asparaginase-loaded hydrogels. BIOMATERIALS SCIENCE. 2025;13(15):4139–52.
- IEEE
- [1]H. Vu et al., “Peptide hydrogels as slow-release formulations of protein therapeutics : case study of asparaginase-loaded hydrogels,” BIOMATERIALS SCIENCE, vol. 13, no. 15, pp. 4139–4152, 2025.
@article{01JYEEC70JBJC947PH4C5NPFN1,
abstract = {{In this study, hexamer peptide-based hydrogels were loaded with different model protein cargos and the
release profiles investigated to explore the balance between injectability and loading capacity permitting
the release of a therapeutically relevant dose. We demonstrate that the release of protein cargos from our
hexamer peptide hydrogels depends on the stability of the hydrogel network, the mobility of the cargo to
diffuse out of the network, and the interaction between the hydrogel network and the cargo. For the first
time, our peptide hydrogels were used to develop an injectable sustained release formulation of a thera-
peutic enzyme, namely Erwinase®, an FDA-approved asparaginase for the treatment of acute lympho-
blastic leukemia. We show that the current hexamer peptide-based hydrogels allow sufficient protein
loading and sustained release of the fully active asparaginase enzyme both in vitro and in vivo. Altogether,
this study describes how peptide hydrogels can be exploited to provide injectable slow-release formu-
lations of biologics, including enzyme therapeutics, to enhance their clinical applicability.}},
author = {{Vu, Hue and Peeters, Evelien and Hofkens, Kenneth and Vandemeulebroecke, Katrien and T'Sas, Sara and Martin, Charlotte and Ballet, Steven and Hoogenboom, Richard and Goossens, Steven and Lammens, Tim and Van Trimpont, Maaike and Madder, Annemieke}},
issn = {{2047-4830}},
journal = {{BIOMATERIALS SCIENCE}},
keywords = {{ERWINIA-CHRYSANTHEMI,DRUG-RELEASE,DELIVERY,DESIGN}},
language = {{eng}},
number = {{15}},
pages = {{4139--4152}},
title = {{Peptide hydrogels as slow-release formulations of protein therapeutics : case study of asparaginase-loaded hydrogels}},
url = {{http://doi.org/10.1039/d5bm00138b}},
volume = {{13}},
year = {{2025}},
}
- Altmetric
- View in Altmetric
- Web of Science
- Times cited: