https://www.cas.cn/syky/202510/t20251020_5085621.shtml

https://www.science.org/doi/10.1126/sciadv.adx7035

Metalloproteins account for approximately one-third or more of the entire proteome and are involved in regulating nearly all biological processes.

A team at the CAS Shanghai Institute of Organic Chemistry has developed a novel cysteine-specific metalloproteome profiling strategy named Cysteine-centered Metalloproteome Profiling (CysMP). This method provides highly sensitive, high-throughput, and specific technical support for deciphering the human metalloproteome and offers an innovative solution for systematic metalloproteome studies.

The researchers have identified a total of 8,895 cysteine ​​metal binding sites, covering 4,150 proteins. These include zinc (Zn2+), copper (Cu2+), calcium (Ca2+), cobalt (Co2+), nickel (Ni2+), manganese (Mn2+), iron (Fe3+ and Fe2+), antimony (Sb3+), chromium (Cr3+), and tin (Sn2+). The study revealed that different metal ions exhibit specificity and preferences in protein binding.

The CysMP strategy provides a systematic resource for studying the relationship between metal ion imbalance, proteomic function, and disease.