Peptides comprising D-amino acids have been shown to be resistant to proteolysis. This makes them potential candidates as probes of cellular interactions, notably protein-biomolecule interactions. However, the empirical conversion of the amino acids that constitute a peptide from L-forms to D-forms will result in abrogation of the normal interactions made by the L-amino acids due to side-chain orientation changes that are associated with the changes in chirality. These interactions can be preserved by reversing the sequence of the D-peptide. We present a web server (http://dstabilize.bii.a-star.edu.sg/) that allows users to convert between L-proteins and D-proteins and for sequence reversal of D-peptides, along with the capability of performing other empirical geometric transforms. This resource allows the user to generate structures of interest easily for subsequent in silico processing.

已显示包含 D-氨基酸的肽对蛋白水解具有抗性。这使它们成为潜在的候选者，作为细胞相互作用的探针，特别是蛋白质-生物分子相互作用。然而，构成肽的氨基酸从 L 型到 D 型的经验转化将导致 L-氨基酸产生的正常相互作用的废除，因为侧链方向的变化与手性。这些相互作用可以通过反转 D 肽的序列来保留。我们提供了一个网络服务器 (http://dstabilize.bii.a-star.edu.sg/)，它允许用户在 L-蛋白质和 D-蛋白质之间进行转换以及 D-肽的序列反转，以及执行其他经验几何变换。硅处理。