Developing Galectin-3-Targeted Therapeutics in Diseases: Three Distinct Galectin-3 Segments for Targeting
Paulina Sindrewicz-Goral, Oluwatobi Adegbite, Jessie Y Yu, Lu-Gang Yu · 2026
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Description
Paulina Sindrewicz-Goral and co-authors review, in a 2026 article, how drug designers might attack galectin-3, a sugar-binding protein implicated in cancer, inflammation, and fibrosis. Inhibitors exist and some have done well in early trials, but every one of them aims at the same canonical binding pocket on the protein's recognition domain, the so-called S-face.
The review maps galectin-3's three-part construction and the distinct jobs of each segment, then argues the target is bigger than one pocket. The opposite F-face of the recognition domain can also bind sugars through a non-canonical interface. The flexible N-terminal tail, unique to galectin-3 among its family, offers a spot rivals cannot cross-react with. Drugs touching several segments at once, or combinations aimed at different segments, could beat single-site blockers, the authors propose.
Catalog record
| CREATOR | Paulina Sindrewicz-Goral, Oluwatobi Adegbite, Jessie Y Yu, Lu-Gang Yu |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 73973 |
| LICENSE | https://creativecommons.org/licenses/by/4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |