Self-Assembling Multidomain Peptide Hydrogels: Designed Susceptibility to Enzymatic Cleavage Allows Enhanced Cell Migration and Spreading
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Multidomain peptides are a class of amphiphilic self-assembling peptides with a modular ABA block motif in which the amphiphilic B block drives self-assembly while the flanking A blocks, which are electrostatically charged, control the conditions under which assembly takes place. Previously we have shown that careful selection of the amino acids in the A and B blocks allow one to control the self-assembled fiber length and viscoelastic properties of formed hydrogels. Here we demonstrate how the modular nature of this peptide assembler can be designed for biological applications. With control over fiber length and diameter, gelation conditions, and viscoelastic properties, we can develop suitable materials for biological applications. Going beyond a simple carrier for cell delivery, a biofunctional scaffold will interact with the cells it carries, promoting advantageous cell-matrix interactions. We demonstrate the design of a multidomain peptide into a bioactive variant by incorporation of a matrix metalloprotease 2 (MMP-2) specific cleavage site and cell adhesion motif. Gel formation and rheological properties were assessed and compared to related peptide hydrogels. Proteolytic degradation by collagenase IV was observed in a gel weight loss study and confirmed by specific MMP-2 degradation monitored by mass spectrometry and cryo-transmission electron microscopy (cryo-TEM). Combination of this cleavage site with the cell adhesion motif RGD resulted in increased cell viability and cell spreading and encouraged cell migration into the hydrogel matrix. Collectively the structural, mechanical, and bioactive properties of this multidomain peptide hydrogel make it suitable as an injectable material for a variety of tissue engineering applications.
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Recombinant proteins can be programmed to degrade and remodel at controlled rates by including protease recognition sites or changing crosslinking chemistry.
“They can be programmed to degrade and remodel at controlled rates by including protease recognition sites206 or changing crosslinking chemistry207.”
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- Authors
- Galler, K. M., Aulisa, L., Regan, K. R., D’Souza, R. N., & Hartgerink, J. D.
- Affiliations
- Texas A&M Health Science Center (US)
- Corresponding author
- Hartgerink, Jeffrey D.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2010-02-16
- Volume
- 132
- Issue
- 9
- Pages
- 3217-3223
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- PMC
- PMC2857986
- OpenAlex
- W2075924474
- Cited by
- 339
- References
- 21
- Citations by year
- 2026: 7 · 2025: 9 · 2024: 11 · 2023: 13 · 2022: 10 · 2021: 17 · 2020: 28 · 2019: 18 · 2018: 20 · 2017: 19 · 2016: 30 · 2015: 40 · 2014: 33 · 2013: 24 · 2012: 15
- FWCI
- 10.81
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of the American Chemical Society (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of Dental and Craniofacial Research (R01DE027255, T32DE018380)
- Division of Materials Research
- Topics
- Physical Sciences › Materials Science › Biomaterials › Supramolecular Self-Assembly in Materials
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Medicine › Hydrogels: synthesis, properties, applications
- Physical Sciences › Materials Science › Biomaterials › Silk-based biomaterials and applications
- Keywords
- self-assembling peptide hydrogel, enzymatic cleavage, MMP-2, collagenase IV, cell migration, cell spreading, injectable scaffolds, tissue engineering, bioactive hydrogels
- MeSH terms
- Cell Adhesion, Cell Movement, Cells, Cultured, Humans, Endopeptidases, Peptides, Tooth, Deciduous, Hydrogels, Cell Size, Cell Proliferation
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