Although b-hairpins are widespread in proteins, there is no tool to coax any small peptide to adopt a b-hairpin conformation, regardless of sequence.H ere,w er eport that dlinked g(R)-methyl-ornithine ( d MeOrn) provides an improved b-turn template for inducing a b-hairpin conformation in peptides.W ed eveloped as ynthesis of protected d MeOrn as ab uilding blocks uitable for use in Fmoc-based solid-phase peptide synthesis.T he synthesis begins with l-leucine and affords gram quantities of the N a -Boc-N d -Fmoc-g(R)-methylornithine building block. X-rayc rystallography confirms that the d MeOrn turn unit adopts afolded structure in amacrocyclic b-hairpin peptide.C Da nd NMR spectroscopya llowc omparison of the d MeOrn turn template to the d-linked ornithine ( d Orn) turn template that we previously introduced and to the popular d-Pro-Gly turn template.T hese studies show that the folding of the d MeOrn turn template is substantially better than that of d Orn and is comparable to d-Pro-Gly.

Although b-hairpins are widespread in proteins, there is no tool to coax any small peptide to adopt a b-hairpin conformation, regardless of sequence.H ere,w er eport that dlinked g(R)-methyl-ornithine ( d MeOrn) provides an improved b-turn template for inducing a b-hairpin conformation in peptides.W ed eveloped as ynthesis of protected d MeOrn as ab uilding blocks uitable for use in Fmoc-based solid-phase peptide synthesis.T he synthesis begins with l-leucine and affords gram quantities of the N a -Boc-N d -Fmoc-g(R)-methylornithine building block. X-rayc rystallography confirms that the d MeOrn turn unit adopts afolded structure in amacrocyclic b-hairpin peptide.C Da nd NMR spectroscopya llowc omparison of the d MeOrn turn template to the d-linked ornithine ( d Orn) turn template that we previously introduced and to the popular d-Pro-Gly turn template.T hese studies show that the folding of the d MeOrn turn template is substantially better than that of d Orn and is comparable to d-Pro-Gly.