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Fmoc‐Compatible Solid‐Phase Peptide Synthesis of Long C‐Terminal Peptide Thioesters
Author(s) -
Sewing Axel,
Hilvert Donald
Publication year - 2001
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/1521-3773(20010917)40:18<3395::aid-anie3395>3.0.co;2-g
Subject(s) - native chemical ligation , ethanethiol , peptide , chemistry , solid phase synthesis , peptide synthesis , cleave , trypsin , combinatorial chemistry , semisynthesis , amino acid , ligation , cysteine , biochemistry , organic chemistry , enzyme , biology , microbiology and biotechnology
AlMe 3 and ethanethiol can be used to cleave peptides directly and efficiently from a variety of commercial resins to give C‐terminal thioesters. Successful synthesis of the 37 amino acid long BPTI 1–37 ‐SEt, an activated fragment used to prepare bovine pancreatic trypsin inhibitor (BPTI; see formula) by native chemical ligation, shows that even thioesters of long peptides of complex composition are accessible using standard resins and 9‐fluorenylmethoxycarbonyl (Fmoc) chemistry.