Bioscience Evidence 2024, Vol.14, No.4, 184-194 http://bioscipublisher.com/index.php/be 189 interactions and Pi-Sigma bonds with α-Pinene (Figure 3A), with a binding energy of -5.17 kcal/mol. Eight amino acid residues of PPARα, Val113, Ile110, Phe105, Phe91, His95, Phe183, Phe94, and Pro184, form Alkyl hydrophobic interactions with β-Caryophyllene (Figure 3B), with a binding energy of -6.56 kcal/mol. Five amino acid residues of the CNR2 protein, Val324, Ile317, Met320, Phe218, and Leu321, form Alkyl hydrophobic interactions with α-Pinene, with a binding energy of -5.61 kcal/mol (Figure 3C). Six amino acid residues of CNR2, Met320, Phe218, Val324, Leu321, Tyr334, and Met220, form Alkyl hydrophobic interactions with β-Caryophyllene, with a binding energy of -7.83 kcal/mol (Figure 3D). Molecular interaction simulations indicate that except for the formation of a Pi-Sigma bond between α-Pinene and PPARα, the other binding sites predominantly involve hydrophobic interactions. Although hydrophobic interactions are relatively weaker compared to hydrogen bonds and other intermolecular forces, Autodock simulations show that the binding energies between these molecules range from -5.17 to -7.83 kcal/mol, suggesting that these interactions can form relatively stable BVOC small molecule-protein complexes. Since the hydrophobic effects on the amino acid chains of proteins play a crucial role in the formation and stabilization of protein tertiary and quaternary structures, the modeled interaction between the BVOCs and these amino acids suggests that hydrophobic interactions may influence the conformation of interacting proteins, thereby affecting protein function. Additionally, these interactions rely mainly on hydrophobic forces, forming a relatively stable but weak binding that is reversible, aligning with the traditional Chinese medicine concept of "flexibility and adaptability," offering a therapeutic advantage in alleviating anxiety and insomnia without causing drug dependence or adverse effects. 3 Concluding Remarks This study identified 28 volatile organic compounds (BVOCs) through GC-MS analysis, with terpenoids accounting for over 99% of the total content, notably α-Pinene (67.313%) and 3-Carene (14.046%) which were significantly higher than other components. These high-content terpenoids are likely the primary active substances responsible for the bioactivity of Cypress cone shells. α-Pinene has been shown in several studies to have sedative and anxiolytic effects (Miyazawa and Yamafuji, 2005), while 3-Carene has been found to improve sleep quality (Woo et al., 2019). Therefore, these key components in Cypress cone shells may play a critical role in alleviating anxiety and insomnia. Figure 3 Docking conformations and binding sites of two compounds with proteins Note: A: PPARα-α-Pinene; B: PPARα-β-caryophyllene; C: CNR2-α-Pinene; D: CNR2-β-caryophyllene
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