Scaffold Hopping Method for Design and Development of Potential Allosteric AKT Inhibitors

Alireza Poustforoosh1

  • 1Medicinal and Natural Products Chemistry Research Center, Shiraz University of Medical Sciences, Shiraz, Iran. alireza110_p@yahoo.com.

Molecular Biotechnology
|October 28, 2024
PubMed

Insights

Researchers designed novel allosteric AKT inhibitors using scaffold hopping for cancer therapy. Three compounds (C6, C20, C16) show superior binding affinity to AKT1 compared to triciribine, warranting further investigation.

Area of Science:

  • Oncology
  • Medicinal Chemistry
  • Computational Biology

Background:

  • Targeting AKT is crucial for cancer therapy, with allosteric inhibitors offering greater specificity.
  • The PI3K/Akt/mTOR pathway is a key target in numerous cancers.

Purpose of the Study:

  • To design novel allosteric AKT inhibitors using a ligand/structure-based pipeline and core hopping.
  • To identify potent AKT1 inhibitors with improved binding affinity and specificity.

Main Methods:

  • Utilized a scaffold hopping approach with FDA-approved kinase inhibitors as cores and triciribine as a template.
  • Employed molecular docking, ADME/T analysis, molecular dynamics (MD) simulations, and binding free energy calculations.
  • Screened compounds against the AKT1 allosteric site.

Main Results:

  • Designed 24 novel allosteric AKT inhibitors.
  • Identified three compounds (C6, C20, C16) with significantly higher binding affinity (docking scores -11 to -13 kcal/mol) than triciribine (-8.6 kcal/mol).
  • MD simulations confirmed targeting of key AKT residues in PH and kinase domains.

Conclusions:

  • Scaffold hopping is effective for developing novel anti-cancer agents.
  • The designed compounds C6, C20, and C16 demonstrate significant potential as AKT1 inhibitors.
  • Further in vitro and in vivo experimental validation is recommended for these promising candidates.

Related Concept Videos

PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a...
3.4K
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
5.7K
Allosteric Regulation01:08

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
57.7K
Structure-Activity Relationships and Drug Design01:28

Structure-Activity Relationships and Drug Design

Drug design is a dynamic field that involves discovering and developing new medications based on specific biological targets. This process heavily relies on structure-activity relationships (SAR) and quantitative structure-activity relationships (QSAR) to guide the design and optimization of efficient drugs.
SAR studies the intricate relationship between a drug's chemical structure and biological activity. It focuses on understanding how modifications to a drug's structure can influence...
622
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
5.7K
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
8.3K