Two Sides of the Same Coin: Transthyretin (TTR) as a Target or Drug Carrier for Drug (Bio)conjugates

Transthyretin (TTR) is a tetrameric protein present in plasma and cerebrospinal fluid that binds to thyroxine (T4) and retinol (vitamin A) to transport them across the blood-retina barrier and to the liver. Mutations on the TTR gene cause destabilization of the tetramer structure leading to misfolded monomers and aggregates, thus triggering several pathologies (i.e., cardiomyopathy and neurodegeneration). The stabilization of TTR tetramer architecture and the silencing of TTR gene expression represent viable therapeutic strategies for amyloidosis. Moreover, the TTR role as a delivery system using drug (bio)conjugates has increasingly been interrogated over the last years to facilitate the transport of different drugs displaying poor pharmacokinetic properties. In this Perspective, we highlight TTR two-faced features as a drug target and carrier, reporting the latest findings in TTR stabilization and its involvement as a drug carrier for the selective drug release on different receptors and cells, thus providing insights for future medicinal chemistry applications.

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Publication Details

Journal
Journal of Medicinal Chemistry
Published
2026-02-02
DOI
https://doi.org/10.1021/acs.jmedchem.5c01560
Primary Topic
Amyloidosis: Diagnosis, Treatment, Outcomes
Type
article
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article

Two Sides of the Same Coin: Transthyretin (TTR) as a Target or Drug Carrier for Drug (Bio)conjugates

Sveva Pelliccia, Marco Fragai, Margherita Brindisi, Pasquale Russomanno
Journal of Medicinal Chemistry
Amyloidosis: Diagnosis, Treatment, Outcomes
article

Two Sides of the Same Coin: Transthyretin (TTR) as a Target or Drug Carrier for Drug (Bio)conjugates

Sveva Pelliccia, Marco Fragai, Margherita Brindisi, Pasquale Russomanno
article en

Abstract

Transthyretin (TTR) is a tetrameric protein present in plasma and cerebrospinal fluid that binds to thyroxine (T4) and retinol (vitamin A) to transport them across the blood-retina barrier and to the liver. Mutations on the TTR gene cause destabilization of the tetramer structure leading to misfolded monomers and aggregates, thus triggering several pathologies (i.e., cardiomyopathy and neurodegeneration). The stabilization of TTR tetramer architecture and the silencing of TTR gene expression represent viable therapeutic strategies for amyloidosis. Moreover, the TTR role as a delivery system using drug (bio)conjugates has increasingly been interrogated over the last years to facilitate the transport of different drugs displaying poor pharmacokinetic properties. In this Perspective, we highlight TTR two-faced features as a drug target and carrier, reporting the latest findings in TTR stabilization and its involvement as a drug carrier for the selective drug release on different receptors and cells, thus providing insights for future medicinal chemistry applications.

Journal of Medicinal ChemistryVol. 69(3)
Federico II University Hospital (IT), Interuniversity Consortium for Magnetic Resonance (IT), University of Florence (IT), University of Naples Federico II (IT)
No poverty
Openalex Percentile: Top 70%
Amyloidosis: Diagnosis, Treatment, Outcomes
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