Abstract
d-Amino acids in peptide linkage are a noteworthy exception from the universal homochirality of proteins and peptides.[1] The first animal peptide that was found to contain a d-amino acid as the second residue was dermorphin, isolated from the skin of a South American tree frog.[2] This peptide binds with high affinity to μ-opiate receptors. The d-residue in this and related amphibian opioid peptides is essential for the biological function, whereas the all-L-isomers lack activity.
Highlights
D-Amino acids in peptide linkage are a noteworthy exception from the universal homochirality of proteins and peptides.[1]
Further studies led to the discovery of additional diastereomeric peptides from numerous sources,[3] which include two components, a natriuretic peptide and a b-defensin, from the venom of the male platypus, a primitive mammal.[4]. All of these peptides contain a single d-amino acid substitution in a well-defined position, which is the second residue of the mature product in all vertebrate peptides known to date
Fire-bellied toads (Bombina variegata, Bombina bombina as well as Bombina orientalis) contain in their skin secretions bombinins H, peptides with antibacterial and hemolytic properties,[6] some of which contain a d-amino acid substitution; both isomers coexist in the skin glands
Summary
D-Amino acids in peptide linkage are a noteworthy exception from the universal homochirality of proteins and peptides.[1]. We synthesized two designed planar substrate analogues and tested their effect on the isomerization reaction catalysed by the frog isomerase.
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