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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 (Weinheim an Der Bergstrasse, Germany)

|March 20, 2024

Summary

We developed expressed protein selenoester ligation (EPSL), a novel method for one-pot protein semi-synthesis. This technique efficiently creates modified proteins like ubiquitinated, lipidated, and phosphorylated variants, even at high dilution.

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 ligation methods face limitations in efficiency and concentration.
Semi-synthesis of complex modified proteins requires robust and versatile techniques.

Purpose of the Study:

To introduce a novel expressed protein selenoester ligation (EPSL) methodology.
To enable efficient one-pot semi-synthesis of modified proteins.
To demonstrate the broad applicability of EPSL for complex protein modifications.

Main Methods:

EPSL utilizes ligation between synthetic selenopeptides and protein aryl selenoesters.
Intein fusion precursors generate protein aryl selenoesters.
In situ chemoselective deselenization affords target proteins.

Main Results:

EPSL allows for one-pot semi-synthesis of modified proteins.
The method is effective at high dilution, overcoming limitations of traditional techniques.
Successfully synthesized ubiquitinated polypeptides, lipidated YPT6 analogues, and phosphorylated Hsp27 variants.

Conclusions:

EPSL is a powerful and versatile technology for protein semi-synthesis.
This methodology facilitates the creation of complex and modified proteins.
EPSL offers a significant advancement in protein engineering and biochemical research.