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Author Spotlight: Advancing Structural and Biochemical Studies of Proteins Through Thermal Shift Assays

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Expressed Protein Selenoester Ligation.

Sameer S Kulkarni¹, Emma E Watson¹, Joshua W C Maxwell¹

¹School of Chemistry and Australian Research Council Centre of Excellence for Innovations in Peptide and Protein Science, The University of Sydney, Sydney, NSW 2006, Australia.

Angewandte Chemie (International Ed. in English)

|February 23, 2022

Summary

We developed expressed protein selenoester ligation (EPSL), a novel method for semi-synthesizing modified proteins in one pot. This technique enables efficient production of complex proteins like ubiquitinated and phosphorylated variants, even at high dilutions.

Keywords:

Expressed Protein Selenoesters Peptides Protein Modifications Protein Semi-Synthesis Proteins

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Area of Science:

Biochemistry
Chemical Biology
Protein Chemistry

Background:

Traditional protein semi-synthesis methods face limitations in efficiency and yield, especially for complex modifications or high dilution conditions.
Intein-mediated protein ligation is a powerful tool, but requires optimization for diverse applications.
Developing novel ligation strategies is crucial for advancing protein engineering and functional studies.

Purpose of the Study:

To introduce a novel expressed protein selenoester ligation (EPSL) methodology for one-pot protein semi-synthesis.
To demonstrate the efficiency and versatility of EPSL for producing modified proteins.
To overcome limitations of traditional ligation methods, particularly at high dilution.

Main Methods:

Development of expressed protein selenoester ligation (EPSL) using synthetic selenopeptides and protein aryl selenoesters.
Generation of protein aryl selenoesters from expressed intein fusion precursors.
In situ chemoselective deselenization for final protein formation.
Application of EPSL for synthesizing ubiquitinated polypeptides, lipidated GTPase YPT6 analogues, and phosphorylated Hsp27 variants.

Main Results:

EPSL enables one-pot semi-synthesis of modified proteins with high efficiency.
The method is effective at high dilution concentrations, overcoming a key limitation of traditional techniques.
Successful synthesis of diverse modified proteins, including ubiquitinated, lipidated, and phosphorylated variants, was achieved.

Conclusions:

Expressed protein selenoester ligation (EPSL) is a robust and versatile methodology for protein semi-synthesis.
EPSL offers significant advantages over traditional ligation methods, particularly for complex or dilute protein preparations.
This technology facilitates the production of challenging protein constructs for further biological investigation.