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

  • Mare Cudic
  • Frank Marí
  • Gregg B. Fields
Conference paper
Part of the Advances in Experimental Medicine and Biology book series (volume 611)

Introduction

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.1These 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...

Keywords

Polypeptide Chain Flash Chromatography Intramolecular Cyclization Potassium Ferrocyanide Lactone Formation 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Notes

Acknowledgments

This work was supported by the Florida Sea Grant College Program (R/LR-MB-18), the National Institutes of Health (GM 066004 to F.M., CA 77402 to G.B.F.), and the FAU Center of Excellence in Biomedical and Marine Biotechnology.

References

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    Pisarewicz, K.; Mora, D.; Pf lueger, F. C; Fields, G. B.; Marí, F. J. Am. Chem. Soc. 2005, 127,6207–6215.CrossRefGoogle Scholar
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    Dangel, B. D.; Johnson, J. A.; Sanies, D. J. Am. Chem. Soc. 2001,123, 8149–8150.CrossRefGoogle Scholar
  3. 3.
    Cudic, M.; Lauer-Fields, J. L.; Fields, G. B. J. Peptide Res. 2005, 65, 272–283.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, LLC 2009

Authors and Affiliations

  • Mare Cudic
    • 1
  • Frank Marí
    • 1
  • Gregg B. Fields
    • 1
  1. 1.Department of Chemistry and BiochemistryFlorida Atlantic UniversityBoca RatonUSA

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