A LEA model peptide protects the function of a red fluorescent protein in the dry state

• Main Authors: Takao Furuki, Tatsuya Niwa, Hideki Taguchi, Rie Hatanaka, Takahiro Kikawada, Minoru Sakurai
• Format: Article
• Language: English
• Published: Elsevier 2019-03-01
• Series: Biochemistry and Biophysics Reports
• Online Access: http://www.sciencedirect.com/science/article/pii/S2405580818302085

We tested whether a short model peptide derived from a group 3 late embryogenesis abundant (G3LEA) protein is able to maintain the fluorescence activity of a red fluorescent protein, mKate2, in the dry state. The fluorescence intensity of mKate2 alone decreased gradually through repeated dehydration-rehydration treatments. However, in the presence of the LEA model peptide, the peak intensity was maintained almost perfectly during such stress treatments, which implies that the three dimensional structure of the active site of mKate2 was protected even under severe desiccation conditions. For comparison, similar experiments were performed with other additives such as a native G3LEA protein, trehalose and BSA, all of whose protective abilities were lower than that of the LEA model peptide. Keywords: LEA protein, Anhydrobiosis, Trehalose, Desiccation tolerance, Dry preservation