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Constructing Cyclic Peptides Using an On-Tether Sulfonium Center
Published on: September 28, 2022
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[Enzymatic cyclization of peptides using immobilized sortase A]
Yao Xue Xue Bao = Acta Pharmaceutica Sinica
|August 4, 2015
Summary
Sortase A (SrtA) enzyme facilitates efficient peptide cyclization. Recombinant SrtA with chitin binding or histidine tags maintains activity, enabling simple synthesis of large cyclic peptides.
Area of Science:
- Biochemistry
- Molecular Biology
- Protein Engineering
Background:
- Peptide cyclization enhances biological activity and stability.
- Sortase A (SrtA) from Staphylococcus aureus is a versatile enzyme for protein modification.
Purpose of the Study:
- To evaluate recombinant SrtA with N-terminal tags for peptide cyclization.
- To assess the impact of tags on SrtA's enzymatic activity.
Main Methods:
- Constructed two SrtA recombinant expression systems with chitin binding domain and/or histidine tags.
- Performed enzymatic kinetics assays to determine transpeptidase activity.
- Utilized immobilized and recycled SrtA for cyclizing synthesized peptides.
Main Results:
- Recombinant SrtA variants retained transpeptidase activity comparable to standard conditions.
- Successful cyclization of peptides containing the LPETG motif was achieved.
- Immobilized and recycled SrtA demonstrated efficiency in peptide synthesis.
Conclusions:
- N-terminal tags do not impede SrtA's enzymatic function.
- SrtA-based cyclization offers a straightforward and efficient method for synthesizing large cyclic peptides.
- This approach holds promise for enzymatic peptide synthesis.
