Probing Secondary Structure

beta-Peptide helix
 

The propensity of both α-amino acid oligomers (>20 residues) and β-amino acid oligomers (>5 residues) to form defined secondary structures both in solution and solid phase is well established.  Work within the Davies group, in collaboration with Dr Tim Claridge, Dr Lorna Smith and Professor George Tranter, seeks to determine the effect of incorporation of structural diversity on the conformational preferences of the corresponding β-peptides.

 beta-Peptide helix
 

Key Publications:

  1. The synthesis and crystal structure of Cbz-[(1R,2S)-ACPC]3-OH: a tripeptide derived from the β-amino acid (1R,2S)-cispentacin
    Davies, S. G.; Siddall, E.; Thompson, A. L.; Thomson, J. E. J. Chem. Crystallogr. 201444, 205 
    [View Journal Page]
  2. A systematic study of the solid state and solution phase conformational preferences of β-peptides derived from C(3)-alkyl substituted transpentacin derivatives
    Abraham, E.; Claridge, T. D. W.; Davies, S. G.; Odell, B.; Roberts, P. M.; Russell, A. J.; Smith, A. D.; Smith, L. J.; Storr, H. R.; Sweet, M. J.; Thompson, A. L.; Thomson, J. E.; Tranter, G. E.; Watkin, D. J. Tetrahedron: Asymmetry 2011, 22, 69 [View Journal Page] 
  3. Crystal structures of dipeptides derived from (1R,2S)-2-aminocyclopentanecarboxylic acid and (1S,2R,3S)-2-amino-3-methylcyclopentane-carboxylic acid
    Abraham, E.; Davies, S. G.; Roberts, P. M.; Thomson, J. E. J. Chem. Crystallogr. 2011, 41, 1722
    [View Journal Page]
  4. A systematic study of the solid state and solution phase conformational preferences of β-peptides derived from transpentacin
    Abraham, E.; Bailey, C. W.; Claridge, T. D. W.; Davies, S. G.; Ling, K. B.; Odell, B.; Rees, T. L.; Roberts, P. M.; Russell, A. J.; Smith, A. D.; Smith, L. J.; Storr, H. R.; Sweet, M. J.; Thompson, A. L.; Thomson, J. E.; Tranter, G. E.; Watkin, D. J. Tetrahedron: Asymmetry 2010, 21, 1797 [View Journal Page]

 

 

 

 

 


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