Design of an elasticized collagen scaffold: A method to induce elasticity in a rigid protein

Luuk R. Versteegden, Henk R. Hoogenkamp, Roger M. Lomme, H. van Goor, Dorien M. Tiemessen, Paul J. Geutjes, Egbert Oosterwijk, Wout F. Feitz, Theo G. Hafmans, Nico Verdonschot, Willeke F. Daamen, Toin H. van Kuppevelt

Research output: Contribution to journalArticleAcademicpeer-review

6 Citations (Scopus)

Abstract

Type I collagen is widely applied as a biomaterial for tissue regeneration. In the extracellular matrix, collagen provides strength but not elasticity under large deformations, a characteristic crucial for dynamic organs and generally imparted by elastic fibers. In this study, a methodology is described to induce elastic-like characteristics in a scaffold consisting of solely type I collagen.
Tubular scaffolds are prepared from collagen fibrils by a casting, molding, freezing and lyophilization process. The lyophilized constructs are compressed, corrugated and subsequently chemically crosslinked with carbodiimide in the corrugated position. This procedure induces elastic-like properties in the scaffolds that could be repeatedly stretched five times their original length for at least 1000 cycles. The induced elasticity is entropy driven and can be explained by the introduction of hydrophobic patches that are disrupted upon stretching thus increasing the hydrophobic-hydrophilic interface. The scaffolds are cytocompatible as demonstrated by fibroblast cell culture.
In conclusion, a new straightforward technique is described to endow unique elastic characteristics to scaffolds prepared from type I collagen alone. Scaffolds may be useful for engineering of dynamic tissues such as blood vessels, ligaments, and lung.
Original languageEnglish
Pages (from-to)277-285
Number of pages9
JournalActa biomaterialia
Volume44
DOIs
Publication statusPublished - 2016

Keywords

  • METIS-320156
  • IR-104330
  • Collagen
  • Biomaterial
  • Elasticity
  • Crosslinking
  • Compression
  • Regenerative medicine

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