Modulating supramolecular assemblies and mechanical properties of engineered protein materials by fluorinated amino acids

Carlo Yuvienco, Haresh T. More, Jennifer S. Haghpanah, Raymond S. Tu, Jin Kim Montclare

Research output: Contribution to journalArticle

Abstract

Here we describe the biosynthesis and characterization of fluorinated protein block polymers comprised of the two self-assembling domains (SADs): elastin (E) and the coiled-coil region of cartilage oligomeric matrix proteins (C). Fluorination is achieved by residue-specific incorporation of p-fluorophenylalanine (pFF) to create pFF-EC, pFF-CE, and pFF-ECE. Global fluorination results in downstream effects on the temperature-dependent secondary structure, supramolecular assembly, and bulk mechanical properties. The impact of fluorination on material properties also differs depending on the orientation of the block configurations as well as the number of domains in the fusion. These studies suggest that integration of fluorinated amino acids within protein materials can be employed to tune the material properties, especially mechanical integrity.

Original languageEnglish (US)
Pages (from-to)2273-2278
Number of pages6
JournalBiomacromolecules
Volume13
Issue number8
DOIs
StatePublished - Aug 13 2012

ASJC Scopus subject areas

  • Bioengineering
  • Biomaterials
  • Polymers and Plastics
  • Materials Chemistry

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