Molecular dynamics simulations were used to investigate the hydration and structure of the tripeptide GPG-NH₂, and the effect of substituting a fluorine or hydroxyl gorup onto one of the C_α positions in the glycinamide portion of the molecule. The fluorinated and hydroxylated peptides both display a slight dehydration of the proline and glycinamide residues and a different conformation of the glycinamide residue backbone than the GPG peptide. These two effects result in a significant decrease in the water-mediated interactions between the Gly1 and glycinamide residues, which had previously been shown to nucleate beta turns in GPG-NH₂.

中文翻译：

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前药GPG-NH ₂及其衍生物的水合结构

分子动力学模拟用于研究三肽GPG-NH的水合和结构₂，氟或羟基取代gorup到的C之一的效果_α在该分子的甘氨酰胺部分位置。与GPG肽相比，氟化和羟基化的肽都显示脯氨酸和甘氨酰胺残基略有脱水，甘氨酰胺残基主链的构象不同。这两种作用导致Gly1和甘氨酰胺残基之间的水介导相互作用显着降低，这先前已显示出可以使GPG-NH _2中的β转角成核。