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ScandiumIII

ABSTRACT: 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 N- and C-terminal 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 Standard UPS1 (48 proteins) were analyzed by MALDI-MS and/or LC-MS. A high cleavage specificity N-terminal to serine and threonine residues was observed.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Equus Caballus (horse) Homo Sapiens (human) Bos Taurus (bovine)

SUBMITTER: Christian Koehler

LAB HEAD: Bernd Thiede

PROVIDER: PXD014918 | Pride | 2020-05-26

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	190104_Sc_A1AG_60C_1.dat	Other
	190104_Sc_A1AG_60C_1.mgf	Mgf
	190104_Sc_A1AG_60C_1.raw	Raw
	190104_Sc_CasB_60C_1.dat	Other
	190104_Sc_CasB_60C_1.mgf	Mgf

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Publications

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

Koehler Christian J CJ Thiede Bernd B

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry 20191030 1

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 ...[more]

PMID: 31667593

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