title: Temperature-triggered phase separation of a hydrophilic resilin-like polypeptide.
abstract: 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.affiliation: Department of Materials Science and Engineering, University of Delaware, Newark, Delaware, 19716, USA.
authors.forename: Linqing
authors.initials: L
authors.lastname: Li
authors.forename: Tianzhi
authors.initials: T
authors.lastname: Luo
authors.forename: Kristi L
authors.initials: KL
authors.lastname: Kiick
mesh_terms: D057927:Hydrophobic and Hydrophilic Interactions; D019476:Insect Proteins / Q000737:chemistry*; D053758:Nanoparticles / Q000737:chemistry / Q000648:ultrastructure; D009391:Nephelometry and Turbidimetry; D044367:Phase Transition; D012996:Solutions
chemical_list: D019476:Insect Proteins; D012996:Solutions; C030951:resilin
keywords: Hofmeister series; nanoparticle; phase transition; protein aggregation; resilin-like polypeptide