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Elastin-Like polypeptides (ELPs), as well-known temperature-controlled bio-macromolecules, are widely used. However, little is known about the interactions between ELPs and macromolecules, which is an important yet neglected problem. Here, the phase transition characteristics of an ELPs-SpyCatcher fusion protein (E-C) in the presence of polyethylene glycol (PEG) in single salts (Na 2 CO 3 , Na 2 SO 4 , NaCl) solutions were investigated using a UV spectrophotometer, DLC, and fluorescence spectroscopy, and we got some interesting results. The phases transition of E-C occurred at a concentration lower than 0.5 mol/L Na 2 CO 3 /PEG2000, while in single Na 2 CO 3 (&lt;0.5 mol/L), the phase transition of E-C did not occur. In the Na 2 CO 3 /PEG solution, we observed a unique two-step phase transition of E-C when the Na 2 CO 3 concentration was 0.5 mol/L and PEG2000 concentration was less than 0.15 g/mL, respectively. In the Na 2 CO 3 /PEG2000 solution, the phase-transition temperature of E-C decreased with the increase of PEG concentration, but increased in the Na 2 SO 4 /PEG2000 solution, while it remained unchanged in the NaCl/PEG2000 solution. However, the phase-transition temperature of the linear ELPs40 decreased under the same salts/PEG2000 solutions. We also addressed the possible molecular mechanism of the interesting results. In contrast to the current well-understood salts-ELPs interactions, this work provides some new insights into the interaction between the PEG-salts-ELPs in solution.

Unique Phase Transition of Exogenous Fusion Elastin-like Polypeptides in the Solution Containing Polyethylene Glycol