Predominant cleavage of proteins N-terminal to serines and threonines using scandium(III) triflate.

ABSTRACT: Proteolytic digestion prior to LC-MS analysis is a key step for the identification of proteins. Digestion of proteins is typically performed with trypsin, but certain proteins or important protein sequence regions might be missed using this endoproteinase. Only few alternative endoproteinases are available and chemical cleavage of proteins is rarely used. Recently, it has been reported that some metal complexes can act as artificial proteases. In particular, the Lewis acid scandium(III) triflate has been shown to catalyze the cleavage of peptide bonds to serine and threonine residues. Therefore, we investigated if this compound can also be used for the cleavage of proteins. For this purpose, several single proteins, the 20S immune-proteasome (17 proteins), and the Universal Proteomics Stan

SUBMITTER: Koehler CJ 

PROVIDER: S-EPMC7064626 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature