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Tunable protein release from a peptide hydrogel

Wednesday, September 13, 2017 — Poster Session I

12:00 p.m. – 1:30 p.m.
FAES Terrace
NCI
CHEMBIO-6

Authors

  • SE Miller
  • Y Yamada
  • S Tau
  • JP Schneider

Abstract

Protein therapeutics have become a significant source of new drugs in recent years due to high affinity and selectivity towards specific biological targets. However, proteins can’t be delivered orally and the need for constant IV injections can complicate patient compliance with treatment regimens. Hydrogels are one type of material that researchers have been attempting to use for improved protein delivery. Over the years our lab has developed a variety of hydrogels composed of self-assembling beta-hairpin peptides with shear-thin recovery properties, making them capable of syringe injection directly to a site of interest. A single, local injection of therapeutic agents encapsulated in gel can have the same efficacy as daily, systemic injections by IV. Here we report an extension of this work to precisely control the rate of protein release from one of our peptide gels. By installing a small fusion tag onto a protein of interest, we can precisely control the rate of protein release from the hydrogel. We have demonstrated a diverse set of release profiles for the model fluorescent protein EGFP, ranging from very fast, to intermediate and very slow. To date, this is the first hydrogel delivery strategy to display such control of protein release without making alterations to the gel itself. This high degree of control over release affords us the ability to tailor our design based on the optimal therapeutic delivery timeline for a specific clinical application.

Category: Chemical Biology