Phase behavior of elastin-like synthetic recombinamers in deep eutectic solvents

Biomacromolecules. 2012 Jul 9;13(7):2029-36. doi: 10.1021/bm300200e. Epub 2012 Jun 8.

Abstract

Deep eutectic solvents promoted the stabilization of the collapsed state of elastin-like recombinamers - and the subsequent formation of aggregates - upon the loss of the structural water molecules involved in hydrophobic hydration. Cryo-etch scanning electron microscopy allowed the observation of these aggregates in neat deep eutectic solvents. The suppression of the lower critical solution temperature transition, observed by differential scanning calorimetry and dynamic light scattering, confirmed the presence of the elastin-like recombinamers in their collapsed state. Actually, the transition from the collapsed to the expanded state was suppressed even after moderate aqueous dilution - for water contents ranging from nil to ca. 45 wt % - and it was only recovered upon further addition of water - above 50 wt %. These features revealed the preferred stabilization of the collapsed state in not only neat deep eutectic solvents but also partially hydrated deep eutectic solvents. We consider that the capability to trigger the lower critical solution temperature transition by partial hydration of deep eutectic solvent may open interesting perspectives for nano(bio)technological applications of elastin-like recombinamers.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Choline / chemistry*
  • Cryoelectron Microscopy
  • Elastin
  • Microscopy, Electron, Scanning
  • Particle Size
  • Peptides / chemistry*
  • Phase Transition
  • Protein Structure, Quaternary
  • Recombinant Proteins / chemistry
  • Solvents / chemistry*
  • Transition Temperature
  • Urea / chemistry*
  • Water / chemistry*

Substances

  • Peptides
  • Recombinant Proteins
  • Solvents
  • Water
  • Urea
  • Elastin
  • Choline