Theoretical structural insights into the snakin/GASA family.

Among the main classes of cysteine-stabilized antimicrobial peptides, the snakin/GASA family has not yet had any structural characterization. Through the combination of ab initio and comparative modeling with a disulfide bond predictor, the three-dimensional structure prediction of snakin-1 is reported here. The structure was composed of two long α-helices with a disulfide pattern of Cys(I)-Cys(IX), Cys(II)-Cys(VII), Cys(III)-Cys(IV), Cys(V)-Cys(XI), Cys(VI)-Cys(XII) and Cys(VIII)-Cys(X). The overall structure was maintained throughout molecular dynamics simulation. Snakin-1 showed a small degree of structural similarity with thionins and α-helical hairpins. This is the first report of snakin-1 structural characterization, shedding some light on the snakin/GASA family.