An Improved Turn Structure for Inducing β-Hairpin Formation in Peptides.

ABSTRACT: Although β-hairpins are widespread in proteins, there is no tool to coax any small peptide to adopt a β-hairpin conformation, regardless of sequence. Here, we report that δ-linked γ(R)-methyl-ornithine (^δ MeOrn) provides an improved β-turn template for inducing a β-hairpin conformation in peptides. We developed a synthesis of protected ^δ MeOrn as a building block suitable for use in Fmoc-based solid-phase peptide synthesis. The synthesis begins with l-leucine and affords gram quantities of the N^α -Boc-N^δ -Fmoc-γ(R)-methyl-ornithine building block. X-ray crystallography confirms that the ^δ MeOrn turn unit adopts a folded structure in a macrocyclic β-hairpin peptide. CD and NMR spectroscopy allow comparison of the ^δ MeOrn turn

SUBMITTER: Li X 

PROVIDER: S-EPMC8490300 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature