グループ3LEAタンパク質のモデルペプチドに関する分子構造及び機能の研究(セミナー「NIAS International Seminar for Cryobiology and Cryotechnology」)

概要

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The primary structure of group-3 late embryogenesis abundant (G3LEA) proteins includes several times repeat of the characteristic 11-mer motif such as AKDGTKEKAGE. To get insights into the roles of the repeat sequence at molecular level, we have examined physicochemical properties of the 22- or 44-mer chemically-synthesized peptides with two or four tandem repeats of the 11-mer motif, whose sequences were derived from the G3LEA proteins originated in several anhydrobiotic organisms. As a result, it was confirmed that the model peptides belong to the family of intrinsically disordered protein as similar to the native G3LEA proteins: they are disordered in water but form α-helices upon drying. The dried model peptides are in the glassy state up to ca 100℃, and thus they play a role in reinforcing the glassy matrix of co-existing sugar, such as trehalose, in the dried state. The dried model peptides also play a role in sequestrating ionic species in the dried state, accompanied by significant backbone conformational changes. Furthermore, the model peptides have protective activity on the aggregation of proteins and membranes induced by the desiccation stress. Taken together, the model peptides are very useful for studying the functional mechanisms of native G3LEA proteins and they are promising as the protective reagents of biological molecules against desiccation stress.
2013-04-15