| Autor: |
Cosottini, Lucrezia, Buzzigoli, Jacopo, Turano, Paola |
| Zdroj: |
European Journal of Inorganic Chemistry; 12/12/2024, Vol. 27 Issue 35, p1-5, 5p |
| Abstrakt: |
The role of solvent‐exposed cysteines as reactive sites for bioconjugation with a variety of metal drugs or fluorescent probes is emerging in the use of human H‐ferritin (HuHf) as a nanocarrier for targeting various tumor cell lines. Here, we have investigated the role of these residues in controlling the structural stability and ferroxidase activity by analyzing the properties of three variants: C90A, C90AC102A, and C130A. Protein folding and cage assembly were unchanged. Ferroxidase activity was also unaffected, indicating that these cysteines are not involved in either the catalytic activity or the overall iron(II) uptake process. For comparison, activity measurements were also performed on two derivatives involving the solvent‐exposed cysteine residues. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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