319008-71-4Relevant academic research and scientific papers
Bip: A C(α)-tetrasubstituted, axially chiral α-amino acid. Synthesis and conformational preference of model peptides
Formaggio, Fernando,Crisma, Marco,Toniolo, Claudio,Tchertanov, Luba,Guilhem, Jean,Mazaleyrat, Jean-Paul,Gaucher, Anne,Wakselman, Michel
, p. 8721 - 8734 (2007/10/03)
By using the recently proposed biphenyl-based, C(α)-tetrasubstituted, cyclic, axially chiral α-amino acid Bip we synthesised by solution methods a large set of model peptides, including the homo-oligomer series, to the pentamer level. All of the peptides were fully characterised and their preferred conformation was assessed in solution by means of a FT-IR absorption and 1H NMR study. Results of X-ray diffraction analyses of two Bip derivatives and a terminally protected tripeptide with the sequence -Gly-Bip-Gly- are also presented. Our findings indicate that Bip tends to support β-turn and 310-helical structures, although in short peptides the fully-extended (C5) conformation would also be populated to some extent. (C) 2000 Elsevier Science Ltd.
