Bioinformatic investigation of Lytechinus variegatus coelomic fluid peptides as multiple oncogenic proteins inhibitors of colorectal cancer

Context: Colorectal cancer (CRC) remains a significant global health challenge despite advances in treatment modalities. The coelomic fluid of Lytechinus variegatus emerges as a rich source of bioactive peptides with the potential as a new therapeutic anticancer agent. Aims: To analyze the toxicity, allergenicity, and potential of L. variegatus coelomic fluid peptides as multitarget inhibitor agents of CRC cancer cells through an in silico study. Methods: Ten peptides from L. variegatus coelomic fluid were processed using UCSF Chimera software to model the three-dimensional structure. ToxinPred and AllerTop web servers were used to analyze the toxicity and allergenicity of peptides, respectively. The 3D structures of EGFR, AKT1, GSK3B, VEGFR2, and JAK3 were retrieved from the PDBJ database. MOE Software was used to perform molecular docking. Results: Peptide 4 binds to the ATP binding pocket of GSK3B protein with the strongest binding affinity value (-8,68 kcal/mol). The docking results between EGFR and peptides showed that peptide 10 binds to the ATP binding pocket with the lowest binding affinity (-9.52 kcal/mol). Peptide 2 binds to the ATP binding pocket of AKT1 with the lowest binding affinity value (-9.16 kcal/mol). Peptide 3 has the lowest binding affinity value of the JAK3 ATP binding pocket (-8,67 kcal/mol). Peptide 7 binds to the ATP binding pocket of VEGFR2 with the strongest binding affinity (-9,67 kcal/mol). Conclusions: The L. variegatus peptides have the potential as multitarget anti-CRC agents by inhibiting the activity of GSK3B, EGFR, AKT1, JAK3, and VEGFR2 proteins through the ATP competitive inhibitor action based on in silico study.