Oral Presentation 10th Australian Peptide Conference 2013

Utility of Peptide Ligation Chemistry for the Chemical Synthesis of Post-Translationally Modified Peptides and Proteins (#81)

Richard J Payne 1 , Brendan L Wilkinson 1 , Yves Hsieh 1 , Lara R Malins 1 , Robert E Thompson 1
  1. The University of Sydney, Camperdown, NSW, Australia

Glycopeptides and glycoproteins are ubiquitous in nature and possess a range of biological activities that make them attractive targets as novel therapeutics and for applications as biomaterials. The difficulty associated with isolating these complex biomolecules in pure form from nature has led to significant research effort directed toward the total chemical synthesis of homogeneous glycopeptides and glycoproteins for biological study.1,2 This talk will highlight the use of novel solid-phase methodologies and chemical ligation strategies for the total chemical synthesis of a range of homogeneous glycopeptides and glycoproteins (up to 19.5 kDa in size). The preparation of homogeneous fish-derived antifreeze glycoproteins,3 chemokine receptor domains4 and potent anti-thrombotic glycoproteins will be described. Structure-activity data has provided important information on the role of glycosylation on the activity of the peptides and proteins and will also be discussed.

  1. Kent, S. B. H.; Chem. Soc. Rev. 2009, 38, 338-351.
  2. Payne, R. J.; Wong, C.-H. Chem. Commun. 2010, 26, 41-43.
  3. Wilkinson, B. L.; Stone, R. S.; Capiccioti, C. J.; Thaysen-Anderson, M.; Matthews, J. M.; Packer, N. H.; Ben, R. N.; Payne, R. J. Angew. Chem. Int. Ed., 2012, 51, 3606-3610.
  4. Taleski, D.; Butler, S. J.; Stone, M. J.; Payne, R. J. Chem. Asian J. 2011, 6, 1316-1320.