Phase transition behavior of elastin-like polypeptides oligomerized with the Foldon domain北大核心CSCD

To investigate the underlying mechanism of the unique phase transition behavior of SpyCatcher-ELPs40 (C-E) and the influence of the oligomerization domain on the phase transition of C-E, we constructed a non-covalent three-armed star oligomerization of C-E-F and E-F by fusing the Foldon (F) domain with SpyCatcher-ELPs40 (C-E) and ELPs40 (E). Results showed that the phase transition temperature of ELPs40 fused with Foldon was higher than that of ELPs120, whereas it was lower than those of ELPs40 and the SpyTag/SpyCatcher-mediated covalent three-armed elastin-like polypeptides (ELPs). This proved that the topology of ELPs could affect their phase transition behaviors. The phase transition temperature of C-E-F was 28.8 ℃ and 35.6 ℃ higher than those of C-E and ELPs40, respectively, although C-E-F had a similar sequence with C-E and ELPs40. When the concentration of NaCl was 0.8 mol/L, the differences in the phase transition temperatures were 41.2 ℃ and 47.1, respectively. We could only observe the phase transition of C-E-F in the Na2CO3 solution with high concentration (≥ 0.7 mol/ L); however, the phase transition could be clearly detected in the Na2SO4 solution, even when the concentration of Na2SO4 was very low. This result was obviously inconsistent with the Hofmeister series. This is the first report of non-linear ELPs that has shown this unique phase transition behavior. The possible reason was related to the charges distributed on the solvent accessible surface and the oligomeric state of C-E-F triggered by the Foldon domain. © 2018 Science Press. All rights reserved.