Jul 2026· Yakugaku Zasshi-journal of The Pharmaceutical Society of Japan· Vol 146 7, pp.
617-624
· 0 citations
Medicine
TL;DR
Recent work on TPD-inducing small molecules is highlighted and an overview of ribonuclease-targeting chimeras that selectively degrade RNA are provided, which represent an area of growing research interest.
Abstract
Targeted protein degradation (TPD) is an emerging approach that selectively eliminates specific proteins using synthetic molecules, such as proteolysis-targeting chimeras (PROTACs). It has attracted increasing attention in medicinal chemistry and chemical biology, with several PROTACs being tested in clinical settings. Unlike traditional small molecules, such as enzyme inhibitors and receptor antagonists, PROTACs exhibit a fundamentally different mechanism. Conventional drugs block enzymatic activities or receptor interactions, whereas PROTACs induce the degradation of target proteins, decreasing their cellular levels and abolishing all associated functions. PROTACs targeting enzymes in protein complexes disrupt both their catalytic activity and involvement in complex formation. In some cases, they also degrade other proteins in complexes, facilitating the elimination of entire assemblies. Our study leverages these unique features of TPD. We are currently developing various PROTACs targeting the enzymes responsible for lysine acetylation or methylation in proteins. Recently, the TPD concept has been extended beyond proteins to include nucleic acids, and ribonuclease-targeting chimeras (RIBOTACs) that selectively degrade RNA have been developed. We are also actively exploring new RNA-targeted degradation strategies. Herein, we highlight our recent work on TPD-inducing small molecules and provide an overview of RIBOTACs, which represent an area of growing research interest.
This thorough analysis investigates the molecular basis of PROTAC technology, tracking its progression from an elegant intellectual notion to a clinically approved treatment platform and provides a detailed survey of the current clinical landscape.
N. Vijaya Lakshmi Reddy, M. Sarika, V. Deepika et al.· International Journal of Adv...· 0 citations
This review summarizes recent advances in chemical protein degradation strategies for neurodegenerative disorders and highlights potential future perspectives of multifunctional PROTACs for therapeutic development.
Pasquale Degennaro, Imane Ghafir El Idrissi, Rosa Purgatorio et al.· Pharmaceuticals· 0 citations
An overview of the developmental trajectory of the TPD field is provided and how diverse modalities can be leveraged to address intracellular, membrane-associated, and extracellular protein targets are discussed.
Yu-bo Zhang, Junwei Fu, Yue Liu et al.· Acta Pharmacologica Sinica· 0 citations
This work reports the first ligand-directed chemical strategy that converts transient PROTAC-mediated ternary complex formation into binary target recognition via post-translational chemical modification of an E3 ligase, and believes it could provide a platform for next-generation targeted protein degraders to overcome the current limitation of PROTAC approach.
Eunbin Park, Jinjoo Jung, Gangasani Jagadeesh Kumar et al.· Bioorganic chemistry (Print)· 0 citations
Protein degrader drugs such as PROTACs are being advanced as therapeutics targeted against oncogenic proteins. During tumorigenesis, oncogenic proteins can become constitutively activated via mechanisms including gene amplification, which increases protein production, and point mutations, which can extend protein half-life. Few experimental studies have addressed how disease-associated changes in target protein homeostasis influence PROTAC activity. We developed orthogonal methods to increase production or enhance stability of β-catenin, an important oncoprotein and target for degrader therapeutics, and used the dTAG system to evaluate the consequences for PROTAC activity. Stabilizing oncogenic missense mutations increase protein expression up to 5-fold but do not alter the PROTAC-imposed minimal steady-state level. In contrast, transcriptional upregulation increases both pre- and post-treatment target levels, revealing a synthesis-dependent ceiling on achievable depletion. Our results highlight distinct constraints on PROTAC activity arising from different mechanisms of oncogene activation, with potential implications for preclinical modeling, drug resistance and personalized medicine.
Evelina Gudauskaitė, Brianda Hernández-Morán, G. Taylor et al.· Cell Chemical Biology· 0 citations
Targeted protein degradation mediated by antibodies has emerged as a promising strategy for degrading extracellular or membrane-bound proteins. Proteolysis-Targeting Antibodies (PROTABs) are bispecific antibodies specifically designed to induce the degradation of membrane proteins by tethering them to a cell surface E3 ligase, which promotes ubiquitination and subsequent degradation. Recent studies have demonstrated the potential of PROTABs to degrade oncogenic receptors, but their underlying mechanisms remain to be fully elucidated. Here, we investigated the mechanism of action of a HER2-targeting PROTAB comprising an anti-Zinc and RING finger protein 3 (ZNRF3) arm and an anti-receptor tyrosine-protein kinase erbB-2 (HER2) arm. We show that PROTAB induces rapid ternary complex formation, followed by receptor internalization and degradation, resulting in ~ 85% target depletion within 24 h. Mechanistically, ubiquitination enhances but is not strictly required for internalization, and degradation proceeds predominantly through the lysosomal pathway. Notably, ZNRF3 is not codegraded but instead accumulates at the cell surface, while the PROTAB antibody itself is largely recycled. Importantly, target degradation does not consistently translate into growth inhibition, highlighting the role of cellular context and target dependency. Together, these findings provide a mechanistic framework for PROTAB function and inform the rational design of next-generation antibody-based degraders.
Jieyan He, Tao Sun, Mengwen Zhang et al.· The FEBS Journal· 0 citations
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