Salt Effects on the structural and thermodynamic properties of a group 3 LEA protein model peptide.

To sequestrate or scavenge ionic species in desiccated cells is one of the putative functions of group 3 late embryogenesis abundant (G3LEA) proteins. We still lack direct physicochemical information on how G3LEA proteins and their characteristic primary amino acid sequences, i.e., 11-mer motif repeats, behave in the presence of salts under water-deficit conditions. In the current study, we investigated salt effects as a function of water content on the structural and thermodynamic properties of the 22-mer peptide (PvLEA-22), consisting of two tandem repeats of the consensus 11-mer motif of G3LEA proteins from the larvae of P. vanderplanki. The results of circular dichroism (CD) and Fourier transform infrared (FT-IR) spectroscopic measurements indicate four main points as follows: (1) PvLEA-22 is in random coils in the aqueous solutions with or without a salt. (2) Dried PvLEA-22, whether salt-free or mixed with NaCl or KCl, is largely folded as α-helix. (3) When dried with MgCl(2) or CaCl(2), PvLEA-22 adopts β-sheet structure as well as random coil. (4) PvLEA-22 faithfully reproduces the conformational changes of the native LEA protein in response to added salts. Furthermore, through temperature-modulated differential scanning calorimetry (TMDSC) measurements, dried PvLEA-22 is found to be in the glassy state at ambient temperatures, independent of which salt is present. On the basis of these results, we discuss the intrinsic nature and putative functional roles of G3LEA proteins under salt-rich conditions.