Structural Insights and Anticancer Potential of Melittin in Cd147 Interaction

Abstract

Objective: This study investigates the interaction between melittin (PDB ID: 2MLT), a bioactive peptide from honeybee venom, and CD147 (PDB ID: 5XF0), a glycosylated transmembrane protein implicated in tumor progression. Material and Method: Employing molecular docking and bioinformatics tools, our structural analysis reveals diverse binding features, including hydrogen bonds, salt bridges, and non-bonded contacts, between the CD147 complex and melittin. Result and Discussion: Non-bonded interactions between 2MLT and specific amino acids (Gly181 and Arg201) of CD147 are highlighted, resembling aspects of the CypA/CD147 binding mechanism (Pro180-Gly181 and Arg201). The elevated anticancer potential of 2MLT was substantiated by utilizing the AntiCP 2.0 server and the ENNAACT server, employing machine learning and artificial neural network algorithms. Additionally, hydrophobicity analysis aligns with characteristics associated with anticancer peptides. Notably, thermodynamic stability variations with temperature underscore the robust binding affinity of 2MLT to the 5XF0 receptor. While our study comprehensively explores molecular interactions and predictive analyses, further in vitro and in vivo investigations are crucial to validate these findings for potential therapeutic applications.