期刊
BIOMATERIALS SCIENCE
卷 1, 期 10, 页码 1037-1045出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c3bm60161g
关键词
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资金
- National Institutes of Health (NIBIB) [1R01EB009701]
- National Institutes of Health (NCI) [U54 CA151880]
- National Science Foundation [CHE-0802286]
- Chicago Biomedical Consortium
- Searle Funds at The Chicago Community Trust
Self-assembled peptide materials have received considerable interest for a range of applications, including 3D cell culture, tissue engineering, and the delivery of cells and drugs. One challenge in applying such materials within these areas has been the extreme stability of beta-sheet fibrillized peptides, which are resistant to proteolysis, degradation, and turnover in biological environments. In this study, we designed self-assembling depsipeptides containing ester bonds within the peptide backbone. Beta-sheet fibrillized nanofibers were formed in physiologic conditions, and two of these nanofiber-forming depsipeptides produced hydrogels that degraded controllably over the course of days-to-weeks via ester hydrolysis. With HPLC, TEM, and oscillating rheometry, we show that the rate of hydrolysis can be controlled in a straightforward manner by specifying the amino acid residues surrounding the ester bond. In 3D cell cultures, depsipeptide gels softened over the course of several days and permitted considerably more proliferation and spreading of C3H10T1/2 pluripotent stem cells than non-degradable analogs. This approach now provides a reliable and reproducible means to soften or clear beta-sheet fibrillized peptide materials from biological environments.
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