Enhancement in the rate of conversion of peptide Cys-Pro esters to peptide thioesters by structural modification |
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Authors: | Toru Kawakami Akitaka KamauchiEmi Harada Saburo Aimoto |
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Affiliation: | Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan |
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Abstract: | We previously reported that the peptide containing a Cys-Pro ester (CPE) moiety is spontaneously transformed into a peptide thioester via an N to S acyl shift followed by diketopiperazine formation. In an attempt to identify more reactive structures for the formation of a peptide thioester, we modified the CPE structure, in which the Pro residue in the CPE moiety was replaced with N-substituted glycine derivatives. These peptides were transformed into a peptide thioester more rapidly. Alternatively, the addition of an amino acid residue at the C-terminus of the CPE moiety also accelerated thioester formation. |
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Keywords: | Chemical ligation CPE peptide Diketopiperazine N&ndash S acyl shift Peptide thioester |
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