One-Pot Cyclization and Cleavage of Peptides with N-Terminal Cysteine via the N,S-Acyl Shift of the N-2-[Thioethyl]glycine Residue | Zendy

Magdalena Wierzbicka | Zendy; Mateusz Waliczek | Zendy; Anna Dziadecka | Zendy; Piotr Stefanowicz | Zendy

Open Access

One-Pot Cyclization and Cleavage of Peptides with N-Terminal Cysteine via the N,S-Acyl Shift of the N-2-[Thioethyl]glycine Residue

Author(s) -

Magdalena Wierzbicka,

Mateusz Waliczek,

Anna Dziadecka,

Piotr Stefanowicz

Publication year - 2021

Publication title -

the journal of organic chemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.2

H-Index - 228

eISSN - 1520-6904

pISSN - 0022-3263

DOI - 10.1021/acs.joc.1c01045

Subject(s) - chemistry , tetrapeptide , cysteine , native chemical ligation , peptide , stereochemistry , cyclic peptide , cleavage (geology) , glycine , residue (chemistry) , epimer , semisynthesis , trypsin , bicyclic molecule , combinatorial chemistry , amino acid , biochemistry , enzyme , geotechnical engineering , fracture (geology) , engineering

We developed a one-pot method for peptide cleavage from a solid support via the N,S -acyl shift of N -2-[thioethyl]glycine and transthioesterification using external thiols to produce cyclic peptides through native chemical self-ligation with the N -terminal cysteine. The feasibility of this methodology is validated by the syntheses of model short peptides, including a tetrapeptide, the bicyclic sunflower trypsin inhibitor SFTI-1, and rhesus Θ-defensin RTD-1. Synthesis of the whole peptide precursor can be fully automated and proceeds without epimerization or dimerization.

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