We are sorry that we made an error in the production of Figure 7. When we viewed the binding results of protein S1PR1 by Molecular Operating Environment (MOE), we opened the protein directly without closing the previous protein. The improper operation resulted in a protein stacking. Thus, the previous Figure 7 depicted wrong binding modes, and we described wrong results accordingly. To correct these issues, a revised paragraph and new Figure 7 are presented below. Figure 7. Binding of fingolimod and berberine to S1PR1 and SPHK1 by Molecular Operating Environment (MOE). Binding results of (A) fingolimod and (B) berberine to S1PR1. Binding results of (C) fingolimod and (D) berberine to SPHK1. Molecules are shown by green atoms, and π–H interactions are shown by dotted green lines. Binding of Fingolimod and Berberine to S1PR1 and Sphingosine Kinase 1 (SPHK1). To identify whether berberine exerts its anti-UC activity through the same target molecule as fingolimod, molecular docking was performed to predict the potential binding modes of berberine to S1PR1 and SPHK1, a signaling kinase that is also involved in the S1P pathway, using the molecular docking of fingolimod for comparison. The results of fingolimod and berberine binding to S1PR1 and SPHK1 are shown in Figure 7. When binding to S1PR1 with the lowest-energy docking pose, fingolimod formed π–H interactions with Leu 297 and Phe 125 (Figure 7A) with a docking score of −10.2209 kcal/mol; berberine formed π–H interactions with Leu 297 and Met 124 (Figure 7B) with a docking score of −6.8364 kcal/mol. These results suggest that berberine binds to S1PR1 via only one of the two binding interactions used by fingolimod. Additionally, the docking score of berberine was higher than that of fingolimod, indicating that berberine has a lower binding activity for S1PR1 than fingolimod. When binding to SPHK1, fingolimod formed π–H interactions with Phe C303, Ile C174, and Phe C288 (Figure 7C) with a docking score of −11.1801 kcal/mol; berberine formed π–H interactions with Phe C303 and Ile C174 (Figure 7D) with a docking score of −10.4432 kcal/mol. This observation suggests that berberine and fingolimod have similar SPHK1 binding modes; these results need to be verified using an in vitro binding affinity assay. This article has not yet been cited by other publications. Figure 7. Binding of fingolimod and berberine to S1PR1 and SPHK1 by Molecular Operating Environment (MOE). Binding results of (A) fingolimod and (B) berberine to S1PR1. Binding results of (C) fingolimod and (D) berberine to SPHK1. Molecules are shown by green atoms, and π–H interactions are shown by dotted green lines.

中文翻译：

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在溃疡性结肠炎临床前模型中以低剂量校正天然生物碱小檗碱和 S1PR 调节剂芬戈莫德组合的抗炎功效

很抱歉我们在图7的制作中犯了错误。当我们通过分子操作环境（MOE）查看蛋白质S1PR1的结合结果时，我们直接打开了蛋白质，没有关闭之前的蛋白质。操作不当导致蛋白质堆积。因此，之前的图 7 描述了错误的绑定模式，我们相应地描述了错误的结果。为了纠正这些问题，下面提供了修改后的段落和新的图 7。图 7. 芬戈莫德和小檗碱通过分子操作环境 (MOE) 与 S1PR1 和 SPHK1 的结合。(A) 芬戈莫德和 (B) 小檗碱与 S1PR1 的结合结果。(C) 芬戈莫德和 (D) 小檗碱与 SPHK1 的结合结果。分子用绿色原子表示，π-H 相互作用用绿色虚线表示。芬戈莫德和小檗碱与 S1PR1 和鞘氨醇激酶 1 (SPHK1) 的结合。为了确定小檗碱是否通过与芬戈莫德相同的靶分子发挥其抗 UC 活性，进行分子对接以预测小檗碱与 S1PR1 和 SPHK1 的潜在结合模式，S1PR1 和 SPHK1 是一种信号激酶，也参与 S1P 通路，使用分子对接芬戈莫德进行比较。芬戈莫德和小檗碱与 S1PR1 和 SPHK1 结合的结果如图 7 所示。当以最低能量对接姿势与 S1PR1 结合时，芬戈莫德与 Leu 297 和 Phe 125 形成 π-H 相互作用（图 7A），对接评分为-10.2209 大卡/摩尔；小檗碱与 Leu 297 和 Met 124（图 7B）形成 π-H 相互作用，对接分数为 -6.8364 kcal/mol。这些结果表明小檗碱仅通过芬戈莫德使用的两种结合相互作用中的一种与 S1PR1 结合。此外，小檗碱的对接评分高于芬戈莫德，表明小檗碱对S1PR1的结合活性低于芬戈莫德。当与 SPHK1 结合时，芬戈莫德与 Phe C303、Ile C174 和 Phe C288 形成 π-H 相互作用（图 7C），对接评分为 -11.1801 kcal/mol；小檗碱与 Phe C303 和 Ile C174 形成 π-H 相互作用（图 7D），对接分数为 -10.4432 kcal/mol。这一观察结果表明小檗碱和芬戈莫德具有相似的 SPHK1 结合模式；这些结果需要使用 小檗碱与 Phe C303 和 Ile C174 形成 π-H 相互作用（图 7D），对接分数为 -10.4432 kcal/mol。这一观察结果表明小檗碱和芬戈莫德具有相似的 SPHK1 结合模式；这些结果需要使用 小檗碱与 Phe C303 和 Ile C174 形成 π-H 相互作用（图 7D），对接分数为 -10.4432 kcal/mol。这一观察结果表明小檗碱和芬戈莫德具有相似的 SPHK1 结合模式；这些结果需要使用体外结合亲和力测定。这篇文章还没有被其他出版物引用。图 7. 芬戈莫德和小檗碱通过分子操作环境 (MOE) 与 S1PR1 和 SPHK1 的结合。(A) 芬戈莫德和 (B) 小檗碱与 S1PR1 的结合结果。(C) 芬戈莫德和 (D) 小檗碱与 SPHK1 的结合结果。分子用绿色原子表示，π-H 相互作用用绿色虚线表示。