Temperature-triggered phase separation of a hydrophilic resilin-like polypeptide.

Academic Article


  • Temperature-triggered phase separation of recombinant proteins has offered substantial opportunities in the design of nanoparticles for a variety of applications. Herein, the temperature-triggered phase separation behavior of a recombinant hydrophilic resilin-like polypeptide (RLP) is described. The transition temperature and sizes of RLP-based nanoparticles can be modulated based on variations in polypeptide concentration, salt identity, ionic strength, pH, and denaturing agents, as indicated via UV-Vis spectroscopy and dynamic light scattering (DLS). The irreversible particle formation is coupled with secondary conformational changes from a random coil conformation to a more ordered β-sheet structure. These RLP-based nanoparticles could find potential use as mechanically-responsive components in drug delivery, nanospring, nanotransducer, and biosensor applications.
  • Authors

  • Li, Linqing
  • Luo, Tianzhi
  • Kiick, Kristi L
  • Status

    Publication Date

  • January 2015
  • Published In


  • Hofmeister series
  • Hydrophobic and Hydrophilic Interactions
  • Insect Proteins
  • Nanoparticles
  • Nephelometry and Turbidimetry
  • Phase Transition
  • Solutions
  • nanoparticle
  • phase transition
  • protein aggregation
  • resilin-like polypeptide
  • Digital Object Identifier (doi)

    Start Page

  • 90
  • End Page

  • 95
  • Volume

  • 36
  • Issue

  • 1