Recombinant resilins with a sequence derived from Drosophila melanogaster are highly pH- and temperature-responsive, exhibiting dual phase-transition behavior characterized by both lower (LCST) and upper critical solution temperatures (UCST). However, no studies have investigated the detailed mechanism of this behavior. Here we report the analysis of temperature-triggered assembly behavior of another recombinant resilin with a similar protein sequence. The aggregation temperature and the size of RLP-based particles are modulated based on the use of various salts, ionic strength, pH and denaturing agents, as indicated by UV-Vis spectroscopy and dynamic light scattering. Changes in the secondary conformation of the polypeptide and particle morphologies were explored via FTIR and TEM. The results clearly demonstrated the conformational change under conditions in which particles were formed, and particle formation that varied reliably with assembly temperature. Resilin-based nanoparticles may find applications in drug delivery and biosensors.

Temperature-triggered assembly properties of a recombinant resilin

248th National Meeting (2014)

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