The effect of the ionic liquid choline chloride (CC) on the conformational dynamics of the intrinsically disordered peptide PILEA-22 of group 3 late embryogenesis abundant (LEA) proteins and the helical peptide AKA2 and was studied via circular dichroism. Circular dichroism data of aqueous solutions of PILEA-22 revealed that the peptide favors a polyproline II (PII) helical structure at low temperature and high CC concentrations and that increasing temperature promotes a gain of α-helical structure. The adoption of PII structure at high CC concentrations may allow the peptide to maintain a high surface area for interaction with solvent molecules. As high CC concentrations may mirror the dessication conditions experienced in vivo for late embryogenesis abundant proteins, these results suggest that the adoption of the PII structure is an important damage preventing measure of LEA proteins. These results are discussed in comparison to the effect of CC on helical peptide AKA2.

Effect of choline chloride on secondary structure conformation for two small peptides: A circular dichroism study

249th National Meeting (2015)

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