Gluing GAP to RAS Mutants: A New Approach to an Old Problem in Cancer Drug Development.

KRAS G12D targeting gluing RAS mutants to GAP pancreatic cancer therapy

Journal

International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791

Informations de publication

Date de publication:
22 Feb 2024
Historique:
received: 19 12 2023
revised: 11 02 2024
accepted: 17 02 2024
medline: 13 3 2024
pubmed: 13 3 2024
entrez: 13 3 2024
Statut: epublish

Résumé

Mutated genes may lead to cancer development in numerous tissues. While more than 600 cancer-causing genes are known today, some of the most widespread mutations are connected to the RAS gene; RAS mutations are found in approximately 25% of all human tumors. Specifically, KRAS mutations are involved in the three most lethal cancers in the U.S., namely pancreatic ductal adenocarcinoma, colorectal adenocarcinoma, and lung adenocarcinoma. These cancers are among the most difficult to treat, and they are frequently excluded from chemotherapeutic attacks as hopeless cases. The mutated KRAS proteins have specific three-dimensional conformations, which perturb functional interaction with the GAP protein on the GAP-RAS complex surface, leading to a signaling cascade and uncontrolled cell growth. Here, we describe a gluing docking method for finding small molecules that bind to both the GAP and the mutated KRAS molecules. These small molecules glue together the GAP and the mutated KRAS molecules and may serve as new cancer drugs for the most lethal, most difficult-to-treat, carcinomas. As a proof of concept, we identify two new, drug-like small molecules with the new method; these compounds specifically inhibit the growth of the PANC-1 cell line with KRAS mutation G12D in vitro and in vivo. Importantly, the two new compounds show significantly lower IC

Identifiants

pubmed: 38473821
pii: ijms25052572
doi: 10.3390/ijms25052572
pii:
doi:

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : National Research, Development and Innovation Office
ID : NKP-2018-1.2.1-NKP-2018-00005

Auteurs

Ivan Ranđelović (I)

KINETO Lab Ltd., 1037 Budapest, Hungary.

Kinga Nyíri (K)

Laboratory of Genome Metabolism and Repair, Institute of Molecular Life Sciences, Research Centre for Natural Sciences, Hungarian Research Network, 1117 Budapest, Hungary.
Department of Applied Biotechnology and Food Science, BME Budapest University of Technology and Economics, 1111 Budapest, Hungary.

Gergely Koppány (G)

Laboratory of Genome Metabolism and Repair, Institute of Molecular Life Sciences, Research Centre for Natural Sciences, Hungarian Research Network, 1117 Budapest, Hungary.
Department of Applied Biotechnology and Food Science, BME Budapest University of Technology and Economics, 1111 Budapest, Hungary.

Marcell Baranyi (M)

KINETO Lab Ltd., 1037 Budapest, Hungary.
Department of Pathology, Forensic and Insurance Medicine, Semmelweis University, 1091 Budapest, Hungary.

József Tóvári (J)

Department of Experimental Pharmacology and the National Tumor Biology Laboratory, National Institute of Oncology, 1122 Budapest, Hungary.

Attila Kigyós (A)

KINETO Lab Ltd., 1037 Budapest, Hungary.

József Tímár (J)

Department of Pathology, Forensic and Insurance Medicine, Semmelweis University, 1091 Budapest, Hungary.

Beáta G Vértessy (BG)

Laboratory of Genome Metabolism and Repair, Institute of Molecular Life Sciences, Research Centre for Natural Sciences, Hungarian Research Network, 1117 Budapest, Hungary.
Department of Applied Biotechnology and Food Science, BME Budapest University of Technology and Economics, 1111 Budapest, Hungary.

Vince Grolmusz (V)

Department of Computer Science, Mathematical Institute, Eötvös Loránd University, 1117 Budapest, Hungary.
Uratim Ltd., 1118 Budapest, Hungary.

Classifications MeSH