ArticleMolecular diversity2025
Design and investigation of novel iridoid-based peptide conjugates for targeting EGFR and its mutants L858R and T790M/L858R/C797S: an in silico study.
Article in Molecular diversity, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed.
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7 authors.
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Abstract
In this work, we designed novel peptide conjugates with plant-based iridoid and lichen-derived depside derivatives to target the wild-type EGFR (WT) and its mutants, L858R and T790M/L858R/C797S triple mutant. These mutations are often expressed in multiple cancers, particularly lung cancer. Specifically, the iridoids included 7-deoxyloganetic acid (7-DGA) and loganic acid (LG), while the depside derivative was sekikaic acid (SK). These compounds are known for their innate anticancer properties and were conjugated with two separate peptide sequences KLPGWSG (K) and YSIPKSS (Y). These sequences have been shown to target EGFR in previous phage display library screening, although the mechanism is unknown. Thus, we created the di-conjugates for dual targeting and investigated their interactions of the di-conjugates and that of the neat peptides with the kinase domain of EGFR (WT) and the two mutants using molecular docking, molecular dynamics (MD) simulations, and MM-GBSA analysis. Docking studies revealed that the (7-DGA)
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