Synthesis and solid-phase application of suitably protected γ-hydroxyvaline building blocks

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Hydroxylated amino acids constitute an important modification in proteins. The best characterized of the post-translationally hydroxylated amino acids are γ-hydroxy-Pro (Hyp) and δ-hydroxy-Lys (Hyl), which are commonly found in collagen. Recently, an unexpected modified residue, γ-hydroxy-D-valine (D-Hyv), was identified within ribosomally expressed polypeptide chains of four conopeptides from the venoms of Conus gladiator and Conus mus.1 These conopeptides were the first known examples of a naturally occurring polypeptide chain containing Hyv. In general, γ-hydroxyamino acids are not that common in nature (except γ-hydroxy-Pro) since a hydroxyl group in the γ-position can undergo intramolecular cyclization to form a lactone, cleaving the peptide bond. The stability of Hyv within conopeptides has been explained by the D-configuration at the α-carbon in conjunction with specific interactions with the surrounding L-amino acids. Given the wide range of neurophysiological respo ...