Selective modification and synchronized fluorescent labeling of N-terminal glycine-containing peptides: new tools to illuminate life science research

Selective modification and synchronized fluorescent labeling of N-terminal glycine-containing peptides: new tools to illuminate life science research


Iipeptides ngabathathi-nxaxheba ababalulekileyo kwimisebenzi yobomi, kunye nohlengahlengiso oluthile kunye nokuleyibheli kubalulekile ekufundeni ulwakhiwo kunye nomsebenzi wazo. Over the past decade, methods have been developed to label glycine on α-carbon. However, these methods require pre-functionalization of glycine, which is not possible for rapid recognition of natural amino acids.In this study, we report the dual activation of the α-methylene of glycine, which distinguishes this glycine from 19 other amino acids.

Technical Advantages

Specific selectivity, utilizing the unique chemical properties of N-terminal glycine to realize its specific reaction with modifying reagents and avoid the interference of other amino acid residues.

  • Universal: Applicable to a wide range of N-terminal glycine-containing peptides, as well as different modification groups and fluorescent dyes.
  • Wide range of applications: Provide a powerful tool for peptide structure and function studies, drug screening, bio-imaging and other fields.


This study provides a method for selective labeling of N-terminal glycine peptides using 1,3-diphenyl 1,3-diones to provide pyrrole-based fluorescent products. It is strictly selective for N-terminal glycine due to the “dual activation” mechanism. It provides a theoretical basis for customized N-glycine-based fluorescence modification and a stability test method for rapid identification of N-terminal glycine-containing peptides.

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