Protein digestion using a cysteine-specific backbone cleavage reagent
Yu-De Chuang, Tsung-Jung Yang, Yu-Chi Chih, Ya-Rong Chen, Po-Cheng Kuo, Cheng-Chih Hsu, Shao-Lun Chiou, John Chu · 2026
Read Protein digestion using a cysteine-specific backbone cleavage reagent by Yu-De Chuang, Tsung-Jung Yang, Yu-Chi Chih, Ya-Rong Chen, Po-Cheng Kuo, Cheng-Chih Hsu, Shao-Lun Chiou, John Chu (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-13306187.txt.
Description
Yu-De Chuang and a team of chemists report in 2026 a reagent that cuts proteins at cysteine, filling a gap in protein analysis tools. Enzymes used for digestion cut at basic, aromatic, or acidic building blocks, but none targeted cysteine. Their reagent attacks the bond just before each cysteine in a protein chain.
Tests on a model peptide mapped reaction speed and best conditions, then a model protein confirmed fit with mass spectrometry workflows. The reaction runs fast in water buffers and gives high yields. It also converts the reactive cysteine tip into a stable ring, removing a separate capping step and adding a distinctive mass tag. That tag makes later data analysis easier. The authors present the reagent as practical for routine proteomics, alone or beside standard enzymes.
Catalog record
| CREATOR | Yu-De Chuang, Tsung-Jung Yang, Yu-Chi Chih, Ya-Rong Chen, Po-Cheng Kuo, Cheng-Chih Hsu, Shao-Lun Chiou, John Chu |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 18 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |