diff --git a/wiki/pages/part.html b/wiki/pages/part.html
index 0a2959794ee7ff6ae0d268244ee5676a1109325c..d932872ed6ea2ea49bd0e720b3f7de8429c39c12 100644
--- a/wiki/pages/part.html
+++ b/wiki/pages/part.html
@@ -178,7 +178,7 @@
             <ol>
               <li>The first type of venom peptide we discovered is MVPs. MVPs are novel venom peptides that lead to the death or paralysis of spider mites through blockage of ion channels. We aim to obtain highly specialized venom peptides through genome mining in <i>P. persimilis</i>, a specialized predator of spider mites. Specifically, we first investigated PpVP1 and PpVP2. With structural prediction results using AlphaFold, we modified the two full length peptides to give more potent, shorter recombinant PpVP1S and PpVP2S.</li>
               <br>
-              <li>Due to the fact that all the MVPs we discovered potentially target Ca<sub>V</sub> channels, we aim to incorporate venom peptides with more diverse molecular targets to suppress potential development of drug resistance in spider mites. Thus, we decide to incorporate SVPs, proteins with numerous disulfide bonds which also functions through binding with ion channels and rapidly modifying ion conductance. Specifically, we incorporated rCtx-4 (targeting NaV channels), Cs1A (targeting Ca<sub>V</sub> channels), and HxTx-Hv1h (targeting both Ca<sub>V</sub> and KV channels). As our toxicity assays suggest, all the venom peptides display significant contact efficacy against spider mites.
+              <li>Due to the fact that all the MVPs we discovered potentially target Ca<sub>V</sub> channels, we aim to incorporate venom peptides with more diverse molecular targets to suppress potential development of drug resistance in spider mites. Thus, we decide to incorporate SVPs, proteins with numerous disulfide bonds which also functions through binding with ion channels and rapidly modifying ion conductance. Specifically, we incorporated rCtx-4 (targeting Na<sub>V</sub> channels), Cs1A (targeting Ca<sub>V</sub> channels), and HxTx-Hv1h (targeting both Ca<sub>V</sub> and K<sub>V</sub> channels). As our toxicity assays suggest, all the venom peptides display significant contact efficacy against spider mites.
               </li>
               <br>
               <li>In order to enable the successful and effective expression of the venom peptides, we introduced the annex of G1M5-SUMO tag, which increases the solubility of the proteins expressed. <i>Galanthus nivalis</i> agglutinin (GNA), a lectin which enhances both oral and contact toxicity of the fusion protein, is also introduced. pET28a is chosen as the vector for our protein expression in <i>E. coli</i>.
@@ -242,7 +242,7 @@
                   </td>
                   <td>Protein coding sequences</td>
                   <td>
-                    SVP targeting the insect NaV channels, leading to death and paralysis.
+                    SVP targeting the insect Na<sub>V</sub> channels, leading to death and paralysis.
                   </td>
                 </tr>
                 <tr>
@@ -264,7 +264,7 @@
                   <td>HxTx-Hv1h</td>
                   <td>Protein coding sequences</td>
                   <td>
-                    SVP targeting the insect Ca<sub>V</sub> and KCa channels, leading to death and paralysis.
+                    SVP targeting the insect Ca<sub>V</sub> and K<sub>Ca</sub> channels, leading to death and paralysis.
                   </td>
                 </tr>
                 <!-- 第11个 -->