3 research outputs found

    Postsynthetic Modification of Unprotected Peptides via <i>S</i>‑Tritylation Reaction

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    Tritylation using trityl alcohol (Trt–OH) in 1,1,1,3,3,3-hexafluoro-2-propanol (HFIP) is a convenient and efficient procedure that can offer <i>S</i>-protection of the Cys located in fully unprotected peptides. The procedure simply requires Trt–OH and HFIP to selectively promote <i>S</i>-tritylation in the presence of peptide nucleophilic functionalities

    Synthesis of Cysteine-Rich Peptides by Native Chemical Ligation without Use of Exogenous Thiols

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    Native chemical ligation (NCL) performed without resorting to the use of thiol additives was demonstrated to be an efficient and effective procedure for synthesizing Cys-rich peptides. This method using tris­(2-carboxyethyl)­phosphine (TCEP) as a reducing agent facilitates the ligation reaction even at the Thr-Cys or Ile-Cys site and enables one-pot synthesis of Cys-rich peptides throughout NCL and oxidative folding

    <i>N</i>‑Sulfanylethyl­aminooxy­butyramide (SEAoxy): A Crypto-Thioester Compatible with Fmoc Solid-Phase Peptide Synthesis

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    An <i>N</i>-sulfanylethyl­amino­oxy­butyramide (SEAoxy) has been developed as a novel thioester equivalent for native chemical ligation. SEAoxy peptide was straightforwardly synthesized by conventional Fmoc solid-phase peptide synthesis without a problem. Moreover, SEAoxy peptide could be directly applied to native chemical ligation owing to the intramolecular <i>N</i>-to-<i>S</i> acyl shift that releases the peptide-thioester <i>in situ</i>. This methodology was successfully applied to the synthesis of two bioactive peptides
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