Formation of the intradimer disulfide bond in human calprotectin maintains metal-withholding function and tunes proteolytic susceptibility
Aurelio Mollo, Emma Y. Cool, Bahar Sakar, Kushol Gupta, Elizabeth M. Nolan · 2026
Read Formation of the intradimer disulfide bond in human calprotectin maintains metal-withholding function and tunes proteolytic susceptibility by Aurelio Mollo, Emma Y. Cool, Bahar Sakar, Kushol Gupta, Elizabeth M. Nolan (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-13277319.txt.
Description
Aurelio Mollo and colleagues examine a chemical link inside calprotectin, a human defence protein, in a 2026 study. Calprotectin starves bacteria by locking away metals they need, a strategy called nutritional immunity. Each of its two subunits holds one sulfur-bearing residue that can pair into a disulfide bond.
The team built a clean supply of the bonded form and tested how it behaves. With calcium present it grouped into four-unit assemblies and stripped several metals from bacterial growth media. Bacteria exposed to it showed signs of iron starvation. The bond also made the protein easier for digestive enzymes to cut, which suggests oxidation helps set the protein's working lifetime.
Catalog record
| CREATOR | Aurelio Mollo, Emma Y. Cool, Bahar Sakar, Kushol Gupta, Elizabeth M. Nolan |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 51 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |