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Divergent behavior of glycosylated threonine and serine derivatives in solid phase peptide synthesis.

ABSTRACT: Solid phase peptide coupling of glycosylated threonine derivatives was systematically evaluated. In contrast to glycosylated serine derivatives which are highly prone to epimerization, glycosylated threonine derivatives produce only negligible amounts of epimerization. Under forcing conditions, glycosylated threonine analogs undergo ?-elimination, rather than epimerization. Mechanistic studies and molecular modeling were used to understand the origin of the differences in reactivity.

SUBMITTER: Zhang Y

PROVIDER: S-EPMC3417326 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature

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Divergent behavior of glycosylated threonine and serine derivatives in solid phase peptide synthesis.

Zhang Yalong Y Muthana Saddam M SM Barchi Joseph J JJ Gildersleeve Jeffrey C JC

Organic letters 20120720 15

Solid phase peptide coupling of glycosylated threonine derivatives was systematically evaluated. In contrast to glycosylated serine derivatives which are highly prone to epimerization, glycosylated threonine derivatives produce only negligible amounts of epimerization. Under forcing conditions, glycosylated threonine analogs undergo β-elimination, rather than epimerization. Mechanistic studies and molecular modeling were used to understand the origin of the differences in reactivity. ...[more]

PMID: 22817697

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