Identification of a candidate PRODH allosteric inhibitor MBTP-15324: modulation of proline metabolite profiles and ECM-associated gene-expression changes in lung cancer cells

Current proline dehydrogenase (PRODH) inhibitors lack scaffold diversity. Through virtual screening, microscale thermophoresis, and molecular dynamics simulations, we identified MBTP-15324 as a candidate novel PRODH allosteric inhibitor (Kd = 1.45 μM). In PRODH-overexpressing lung cancer cells (A549 and LLC), MBTP-15324 significantly attenuated cell viability, colony formation, and migration. Furthermore, multi-omics analyses revealed that this putative inhibitor partially reversed arginine-proline metabolic dysregulation and downregulated transcriptional programs associated with inflammation, cell adhesion, and the extracellular matrix (ECM). In conclusion, MBTP-15324 provides a novel-scaffold chemical starting point for future PRODH-targeted therapies and metabolic interventions in lung cancer.

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Journal
Journal of Enzyme Inhibition and Medicinal Chemistry
Published
2026-08-24
DOI
https://doi.org/10.1080/14756366.2026.2719719
Primary Topic
Peptidase Inhibition and Analysis
Type
article
Field-Weighted Citation Impact
0.00

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article

Identification of a candidate PRODH allosteric inhibitor MBTP-15324: modulation of proline metabolite profiles and ECM-associated gene-expression changes in lung cancer cells

Chunqiong Li, Yonglong Han, Cheng Guo, Mengyao Chen et al.
Journal of Enzyme Inhibition and Medicinal Chemistry
Peptidase Inhibition and Analysis
article

Identification of a candidate PRODH allosteric inhibitor MBTP-15324: modulation of proline metabolite profiles and ECM-associated gene-expression changes in lung cancer cells

Chunqiong Li, Yonglong Han, Cheng Guo, Mengyao Chen, Quanjun Yang, Ciqin Li, Yuxuan Zhou, Dingyuan Bai, Zhihan Li, Jun Yan
article en

Abstract

Current proline dehydrogenase (PRODH) inhibitors lack scaffold diversity. Through virtual screening, microscale thermophoresis, and molecular dynamics simulations, we identified MBTP-15324 as a candidate novel PRODH allosteric inhibitor (Kd = 1.45 μM). In PRODH-overexpressing lung cancer cells (A549 and LLC), MBTP-15324 significantly attenuated cell viability, colony formation, and migration. Furthermore, multi-omics analyses revealed that this putative inhibitor partially reversed arginine-proline metabolic dysregulation and downregulated transcriptional programs associated with inflammation, cell adhesion, and the extracellular matrix (ECM). In conclusion, MBTP-15324 provides a novel-scaffold chemical starting point for future PRODH-targeted therapies and metabolic interventions in lung cancer.

Journal of Enzyme Inhibition and Medicinal ChemistryVol. 41(1)
Beijing University of Chinese Medicine (CN), Donghua University (CN), Peking University (CN), Shanghai Sixth People's Hospital (CN), Institute of Molecular Medicine (IN), Shanghai Ocean University (CN)
National Natural Science Foundation of China
Good health and well-being
Openalex Percentile: Top 13%
Peptidase Inhibition and Analysis
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Identification of a candidate PRODH allosteric inhibitor MBTP-15324: modulation of proline metabolite profiles and ECM-associated gene-expression changes in lung cancer cells — Chunqiong Li, Yonglong Han, et al. · Journal of Enzyme Inhibition and Medicinal Chemistry (2026) | TGRS Research Map | TGRS