The effect of choline chloride on the conformational dynamics of two different 11-mer repeat units of group 3 late embryogenesis abundant proteins was studied. Circular dichroism data of aqueous solutions of the peptides, PILEA-22 (AADGAKEKAGE)2 and a consensus sequence (TAQAAKEKAGE)2 revealed that the peptides favor a polyproline II helix structure at low temperature and high choline chloride concentrations and that increasing temperature promotes a gain of α-helical structure. The adoption of polyproline II (PII) structure at high choline chloride concentrations may allow the peptides to maintain a high surface area for interaction with solvent. Additionally, the PILEA-22 peptide is sensitive to the presence of Fe3+ in solution, as supported by the increase in PII helical content at low concentrations of FeCl3, whereas the consensus sequence showed no change in conformational preference with the addition of the salt. As choline chloride has been suggested to improve dessication tolerance, these results support that the adoption of the PII structure is an important damage preventing measure of LEA proteins.

Investigating the effect of choline chloride and trivalent cations on late embryogenesis abundant protein consensus sequences

254th National Meeting (2017)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.