Exploration of a Novel ICMT Inhibitor with More Solubility than Cysmethynil against Membrane Localization of KRAS Mutant in Colorectal Cancer.

Background: ICMT (isoprenylcysteine carboxyl methyltransferase) is an enzyme that plays a key role in the post-translational modification of the K-Ras protein. The carboxyl methylation of this protein by ICMT is important for its proper localization and function. Cysmethynil (2-[5-(3-methylphenyl)-l-octyl-lH-indolo-3-yl] acetamide) causes K-Ras mislocalization and interrupts pathways that control cancer cell growth and division through inhibition of ICMT, but its poor water solubility makes it difficult and impractical for clinical use.

Exploration of Novel PDEδ Inhibitor Based on Pharmacophore and Molecular Docking against KRAS Mutant in Colorectal Cancer.

Aim: The prenyl-binding protein, phosphodiesterase-δ (PDEδ), is essential for the localization of prenylated KRas to the plasma membrane for its signaling in cancer.

Introduction: The general objective of this work was to develop virtually new potential inhibitors of the PDEδ protein that prevent Ras enrichment at the plasma membrane.

Methods: All computational molecular modeling studies were performed by Molecular Operating Environment (MOE).

Withdrawal Notice: Identification of the Interaction between Angiotensin-converting Enzyme Residues and Severe Acute Respiratory Syndrome Coronavirus 2.

Unlabelled: The article has been withdrawn by the Editorial office of the journal Current Pharmaceutical Design. The decision is reached by all authors, for below reasons: • Data been published should be updated. • New approach of this study and new results mentioning the vaccine and its interaction with ACE2.