Structural and Biophysical Characterization of C‐Glycosylic 1,2‐Thiodisaccharides Reveals Determinants of Selective Binding to Galectin‐7 and Galectin‐8N
Anastasia S Tsagkarakou, Anastassia L Kantsadi, Vasiliki I Theodoridou, Nikolaos Veliotis, László Lázár, János József, László Juhász, George Kontopidis, Hakon Leffler, Ulf J Nilsson, László Somsák, Demetres D Leonidas · 2026
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Description
Tsagkarakou and a team in Greece and Hungary mapped in 2026 how sugar like drugs can tell two near twin proteins apart. The proteins, galectin-7 and galectin-8N, grip sugars on cell skins and feed cancer growth and swelling. Their grip pockets look near the same, so drugs tend to hit both. The team built a set of twin sugar chains, linked by sulfur and carbon in place of the usual oxygen, and gauged how each one binds.
One chain, number 17, gripped galectin-8N the best of the set, tighter than the field's base drug. A mate, number 13, leaned the other way, toward galectin-7. Glow tests, heat gauges, and X-ray shots of the bound pairs showed why. The first sugar locks in a stiff nest of bonds in both proteins. The second sugar swings to a split pose in each pocket, and that swing sets the lean.
Catalog record
| CREATOR | Anastasia S Tsagkarakou, Anastassia L Kantsadi, Vasiliki I Theodoridou, Nikolaos Veliotis, László Lázár, János József, László Juhász, George Kontopidis, Hakon Leffler, Ulf J Nilsson, László Somsák, Demetres D Leonidas |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 42 KB |
| LICENSE | https://creativecommons.org/licenses/by/4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |