4.7 Article

Proteolytic stability of amphipathic peptide hydrogels composed of self-assembled pleated β-sheet or coassembled rippled β-sheet fibrils

Journal

CHEMICAL COMMUNICATIONS
Volume 50, Issue 70, Pages 10133-10136

Publisher

ROYAL SOC CHEMISTRY
DOI: 10.1039/c4cc04644g

Keywords

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Funding

  1. University of Rochester Provost's Multidisciplinary Award
  2. National Science Foundation [DMR-1148836]
  3. [CHE-0840410]
  4. [CHE-0946653]
  5. Division Of Materials Research
  6. Direct For Mathematical & Physical Scien [1148836] Funding Source: National Science Foundation

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Hydrogel networks composed of rippled beta-sheet fibrils of coassembled D- and L-Ac-(FKFE)(2)-NH2 amphipathic peptides exhibit proteolytic stability and increased rheological strength compared to networks of self-assembled L-Ac-(FKFE)(2)-NH2 pleated beta-sheet fibrils. Modifying the ratios of L and D peptides in the coassembled rippled beta-sheet fibrils alters the degradation profiles of these hydrogel networks.

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