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Realizing serine/threonine ligation: scope and limitations and mechanistic implication thereof
Clarence T T Wong1, Tianlu Li1, Hiu Yung Lam1
1Department of Chemistry, The University of Hong Kong Hong Kong, China ; State Key Laboratory of Synthetic Chemistry, University of Hong Kong Hong Kong, China.
Frontiers in Chemistry
|June 7, 2014
Summary
Serine/Threonine ligation (STL) is a versatile tool for protein synthesis and bioconjugation. This study confirms STL
Area of Science:
- Chemical Biology
- Synthetic Chemistry
- Biochemistry
Background:
- Serine/Threonine ligation (STL) is a valuable method for protein synthesis and bioconjugation.
- Its application is widespread due to the prevalence of Ser/Thr residues in natural peptides and proteins.
Purpose of the Study:
- To investigate the compatibility of the STL strategy with all 20 natural amino acids at X-Ser/Thr ligation sites.
- To assess the chemoselectivity of STL with internal lysine residues.
Main Methods:
- Systematic evaluation of STL ligation efficiency with various amino acids preceding Ser/Thr.
- Analysis of reaction kinetics and chemoselectivity using salicylaldehyde (SAL) esters.
Main Results:
- STL is compatible with 17 out of 20 natural amino acids at X-Ser/Thr sites.
- Bulky amino acids (Thr, Val, Ile) do not impede ligation rates under current conditions.
- Internal lysine amino groups do not interfere with the STL reaction rate.
Conclusions:
- The STL strategy demonstrates broad amino acid compatibility, enhancing its utility in chemical biology.
- STL offers a chemoselective and efficient ligation method for peptide and protein synthesis.
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