Insights into the Mechanism and Catalysis of Peptide Thioester Synthesis by Alkylselenols Provide a New Tool for Chemical Protein Synthesis

While thiol-based catalysts are widely employed for chemical protein synthesis relying on peptide thioester chemistry, this is less true for selenol-based catalysts whose development is in its infancy. In this study, we compared different selenols derived from the selenocysteamine scaffold for their capacity to promote thiol–thioester exchanges in water at mildly acidic pH and the production of peptide thioesters from bis(2-sulfanylethyl)amido (SEA) peptides. The usefulness of a selected selenol compound is illustrated by the total synthesis of a biologically active human chemotactic protein, which plays an important role in innate and adaptive immunity.

Insights into the Mechanism and Catalysis of Peptide Thioester Synthesis by Alkylselenols Provide a New Tool for Chemical Protein Synthesis

While thiol-based catalysts are widely employed for chemical protein synthesis relying on peptide thioester chemistry, this is less true for selenol-based catalysts whose development is in its infancy. In this study, we compared different selenols derived from the selenocysteamine scaffold for their capacity to promote thiol-thioester exchanges in water at mildly acidic pH and the production of peptide thioesters from bis(2-sulfanylethyl)amido (SEA) peptides. The usefulness of a selected selenol compound is illustrated by the total synthesis of a biologically active human chemotactic protein, which plays an important role in innate and adaptive immunity<br>

Insights into the Mechanism and Catalysis of Peptide Thioester Synthesis by Alkylselenols Provide a New Tool for Chemical Protein Synthesis

While thiol-based catalysts are widely employed for chemical protein synthesis relying on peptide thioester chemistry, this is less true for selenol-based catalysts whose development is in its infancy. In this study, we compared different selenols derived from the selenocysteamine scaffold for their capacity to promote thiol-thioester exchanges in water at mildly acidic pH and the production of peptide thioesters from bis(2-sulfanylethyl)amido (SEA) peptides. The usefulness of a selected selenol compound is illustrated by the total synthesis of a biologically active human chemotactic protein, which plays an important role in innate and adaptive immunity<br>

Palladium mediated deallylation in fully aqueous conditions for native chemical ligation at aspartic and glutamic acid sites

An efficient native chemical ligation approach at Asp and Glu sites is reported applying a hydrazide precursor, as a peptide thioester, and allyl protection at the side chain of Asp and Glu.

Preparation of Peptide o-Aminoanilides Using a Modified Dawson's Linker for Microwave-Assisted Peptide Synthesis

Based on the structure of Dawson’s 3,4-diaminobenzoic acid (Dbz) linker designed for Fmoc solid-phase peptide-thioester synthesis, the 4-amino-3-nitrobenzoic acid [Dbz(NO2)] linker was developed for microwave-assisted synthesis. The Dbz(NO2) linker can be readily converted into the Dbz linker by on-resin reduction with SnCl2 after construction of the protected peptide resin. Although epimerization of C-terminal amino acid restricts the use of Dbz(NO2) linker to the synthesis of peptide-Gly-thioester, use of this linker can prevent side reactions that arise when Dbz or Dbz(Aloc) linkers are used in the microwave-assisted synthesis of Gly-rich peptides.

Serine promoted synthesis of peptide thioester-precursor on solid support for native chemical ligation

Fmoc solid phase peptide synthesis of peptide thioesters by displacement of the cyclic urethane moiety obtained by the selective activation of C-terminal serine.