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Direct arginine modification in native peptides and application to chemical probe development.

ABSTRACT: An efficient method for the direct labeling of the Arg guanidinium group in native peptides is reported. This straightforward procedure allows modifying the arginine moiety in peptides with various reporter groups, such as fluorophores, biotin, etc., under mild conditions in an operationally simple procedure. The scope of this method tolerates various functionalized amino acids such as His, Ser, Trp, Tyr, Glu, etc., while the only limitations uncovered so far are restricted to cysteine and free amine residues. The utility of this late-stage diversification method was demonstrated in direct labeling of leuprolide, a clinically used drug, for distribution monitoring in Daphnia, and in labeling of microcystin, a cyanobacterial toxin.

SUBMITTER: Grundler V

PROVIDER: S-EPMC4265810 | biostudies-other | 2014 Dec

REPOSITORIES: biostudies-other

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Direct arginine modification in native peptides and application to chemical probe development.

Grundler Verena V Gademann Karl K

ACS medicinal chemistry letters 20141027 12

An efficient method for the direct labeling of the Arg guanidinium group in native peptides is reported. This straightforward procedure allows modifying the arginine moiety in peptides with various reporter groups, such as fluorophores, biotin, etc., under mild conditions in an operationally simple procedure. The scope of this method tolerates various functionalized amino acids such as His, Ser, Trp, Tyr, Glu, etc., while the only limitations uncovered so far are restricted to cysteine and free ...[more]

PMID: 25516786

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