Long-term biostability of self-assembling protein polymers in the absence of covalent crosslinking.
Biomaterials
; 31(4): 779-91, 2010 Feb.
Article
em En
| MEDLINE
| ID: mdl-19854505
ABSTRACT
Unless chemically crosslinked, matrix proteins, such as collagen or silk, display a limited lifetime in vivo with significant degradation observed over a period of weeks. Likewise, amphiphilic peptides, lipopeptides, or glycolipids that self-assemble through hydrophobic interactions to form thin films, fiber networks, or vesicles do not demonstrate in vivo biostability beyond a few days. We report herein that a self-assembling, recombinant elastin-mimetic triblock copolymer elicited minimal inflammatory response and displayed robust in vivo stability for periods exceeding 1 year, in the absence of either chemical or ionic crosslinking. Specifically, neither a significant inflammatory response nor calcification was observed upon implantation of test materials into the peritoneal cavity or subcutaneous space of a mouse model. Moreover, serial quantitative magnetic resonance imaging, evaluation of pre- and post-explant ultrastructure by cryo-high resolution scanning electron microscopy, and an examination of implant mechanical responses revealed substantial preservation of form, material architecture, and biomechanical properties, providing convincing evidence of a non-chemically or ionically crosslinked protein polymer system that exhibits long-term stability in vivo.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Polímeros
/
Materiais Biocompatíveis
/
Elastina
Limite:
Animals
Idioma:
En
Ano de publicação:
2010
Tipo de documento:
Article