Biomolecular hydrogels formed and degraded via site-specific enzymatic reactions

Martin Ehrbar, Simone C. Rizzi, Ronald G. Schoenmakers, Blanca San Miguel, J. A. Hubbell, Franz E. Weber, Matthias P. Lutoff

Research output: Contribution to journalArticle

188 Citations (Scopus)

Abstract

We present polymeric hydrogel biomaterials that are biomimetic both in their synthesis and degradation. The design of oligopeptide building blocks with dual enzymatic responsiveness allows us to create polymer networks that are formed and functionalized via enzymatic reactions and are degradable via other enzymatic reactions, both occurring under physiological conditions. The activated transglutaminase enzyme factor XIIIa was utilized for site-specific coupling of prototypical cell adhesion ligands and for simultaneous cross-linking of hydrogel networks from factor XIIIa substrate-modified multiarm poly(ethylene glycol) macromers. Ligand incorporation is nearly quantitative and thus controllable, and does not alter the network's macroscopic properties over a concentration range that elicits specific cell adhesion. Living mammalian cells can be encapsulated in the gels without any noticeable decrease in viability. The degradation of gels can be engineered to occur, for example, via cell-secreted matrix metalloproteinases, thus rendering these gels interesting for biomedical applications such as drug delivery systems or smart implants for in situ tissue engineering.

Original languageEnglish
Pages (from-to)3000-3007
Number of pages8
JournalBiomacromolecules
Volume8
Issue number10
DOIs
StatePublished - Oct 1 2007
Externally publishedYes

Fingerprint

Hydrogels
Factor XIIIa
Gels
Hydrogel
Cell adhesion
Cell Adhesion
Secreted Matrix Metalloproteinases
Ligands
Degradation
Oligopeptides
Biomimetics
Transglutaminases
Ethylene Glycol
Biocompatible Materials
Drug Delivery Systems
Tissue Engineering
Tissue engineering
Biomaterials
Polyethylene glycols
Polymers

ASJC Scopus subject areas

  • Organic Chemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Polymers and Plastics
  • Materials Chemistry

Cite this

Ehrbar, M., Rizzi, S. C., Schoenmakers, R. G., San Miguel, B., Hubbell, J. A., Weber, F. E., & Lutoff, M. P. (2007). Biomolecular hydrogels formed and degraded via site-specific enzymatic reactions. Biomacromolecules, 8(10), 3000-3007. https://doi.org/10.1021/bm070228f

Biomolecular hydrogels formed and degraded via site-specific enzymatic reactions. / Ehrbar, Martin; Rizzi, Simone C.; Schoenmakers, Ronald G.; San Miguel, Blanca; Hubbell, J. A.; Weber, Franz E.; Lutoff, Matthias P.

In: Biomacromolecules, Vol. 8, No. 10, 01.10.2007, p. 3000-3007.

Research output: Contribution to journalArticle

Ehrbar, M, Rizzi, SC, Schoenmakers, RG, San Miguel, B, Hubbell, JA, Weber, FE & Lutoff, MP 2007, 'Biomolecular hydrogels formed and degraded via site-specific enzymatic reactions', Biomacromolecules, vol. 8, no. 10, pp. 3000-3007. https://doi.org/10.1021/bm070228f
Ehrbar M, Rizzi SC, Schoenmakers RG, San Miguel B, Hubbell JA, Weber FE et al. Biomolecular hydrogels formed and degraded via site-specific enzymatic reactions. Biomacromolecules. 2007 Oct 1;8(10):3000-3007. https://doi.org/10.1021/bm070228f
Ehrbar, Martin ; Rizzi, Simone C. ; Schoenmakers, Ronald G. ; San Miguel, Blanca ; Hubbell, J. A. ; Weber, Franz E. ; Lutoff, Matthias P. / Biomolecular hydrogels formed and degraded via site-specific enzymatic reactions. In: Biomacromolecules. 2007 ; Vol. 8, No. 10. pp. 3000-3007.
@article{f938f11c8c4c44cfac6ac9bebec2cf0d,
title = "Biomolecular hydrogels formed and degraded via site-specific enzymatic reactions",
abstract = "We present polymeric hydrogel biomaterials that are biomimetic both in their synthesis and degradation. The design of oligopeptide building blocks with dual enzymatic responsiveness allows us to create polymer networks that are formed and functionalized via enzymatic reactions and are degradable via other enzymatic reactions, both occurring under physiological conditions. The activated transglutaminase enzyme factor XIIIa was utilized for site-specific coupling of prototypical cell adhesion ligands and for simultaneous cross-linking of hydrogel networks from factor XIIIa substrate-modified multiarm poly(ethylene glycol) macromers. Ligand incorporation is nearly quantitative and thus controllable, and does not alter the network's macroscopic properties over a concentration range that elicits specific cell adhesion. Living mammalian cells can be encapsulated in the gels without any noticeable decrease in viability. The degradation of gels can be engineered to occur, for example, via cell-secreted matrix metalloproteinases, thus rendering these gels interesting for biomedical applications such as drug delivery systems or smart implants for in situ tissue engineering.",
author = "Martin Ehrbar and Rizzi, {Simone C.} and Schoenmakers, {Ronald G.} and {San Miguel}, Blanca and Hubbell, {J. A.} and Weber, {Franz E.} and Lutoff, {Matthias P.}",
year = "2007",
month = "10",
day = "1",
doi = "10.1021/bm070228f",
language = "English",
volume = "8",
pages = "3000--3007",
journal = "Biomacromolecules",
issn = "1525-7797",
publisher = "American Chemical Society",
number = "10",

}

TY - JOUR

T1 - Biomolecular hydrogels formed and degraded via site-specific enzymatic reactions

AU - Ehrbar, Martin

AU - Rizzi, Simone C.

AU - Schoenmakers, Ronald G.

AU - San Miguel, Blanca

AU - Hubbell, J. A.

AU - Weber, Franz E.

AU - Lutoff, Matthias P.

PY - 2007/10/1

Y1 - 2007/10/1

N2 - We present polymeric hydrogel biomaterials that are biomimetic both in their synthesis and degradation. The design of oligopeptide building blocks with dual enzymatic responsiveness allows us to create polymer networks that are formed and functionalized via enzymatic reactions and are degradable via other enzymatic reactions, both occurring under physiological conditions. The activated transglutaminase enzyme factor XIIIa was utilized for site-specific coupling of prototypical cell adhesion ligands and for simultaneous cross-linking of hydrogel networks from factor XIIIa substrate-modified multiarm poly(ethylene glycol) macromers. Ligand incorporation is nearly quantitative and thus controllable, and does not alter the network's macroscopic properties over a concentration range that elicits specific cell adhesion. Living mammalian cells can be encapsulated in the gels without any noticeable decrease in viability. The degradation of gels can be engineered to occur, for example, via cell-secreted matrix metalloproteinases, thus rendering these gels interesting for biomedical applications such as drug delivery systems or smart implants for in situ tissue engineering.

AB - We present polymeric hydrogel biomaterials that are biomimetic both in their synthesis and degradation. The design of oligopeptide building blocks with dual enzymatic responsiveness allows us to create polymer networks that are formed and functionalized via enzymatic reactions and are degradable via other enzymatic reactions, both occurring under physiological conditions. The activated transglutaminase enzyme factor XIIIa was utilized for site-specific coupling of prototypical cell adhesion ligands and for simultaneous cross-linking of hydrogel networks from factor XIIIa substrate-modified multiarm poly(ethylene glycol) macromers. Ligand incorporation is nearly quantitative and thus controllable, and does not alter the network's macroscopic properties over a concentration range that elicits specific cell adhesion. Living mammalian cells can be encapsulated in the gels without any noticeable decrease in viability. The degradation of gels can be engineered to occur, for example, via cell-secreted matrix metalloproteinases, thus rendering these gels interesting for biomedical applications such as drug delivery systems or smart implants for in situ tissue engineering.

UR - http://www.scopus.com/inward/record.url?scp=35548972427&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=35548972427&partnerID=8YFLogxK

U2 - 10.1021/bm070228f

DO - 10.1021/bm070228f

M3 - Article

C2 - 17883273

AN - SCOPUS:35548972427

VL - 8

SP - 3000

EP - 3007

JO - Biomacromolecules

JF - Biomacromolecules

SN - 1525-7797

IS - 10

ER -