Encyclopedia

  • The relevance of the relative configuration in the folding of hybrid peptides containing β-cyclobutane amino acids and γ-amino-l-proline residues
  • Add time:08/16/2019         Source:sciencedirect.com

    Four new series of diastereomeric β,γ-di- and β,γ-tetrapeptides derived from conveniently protected (1R,2S)- and (1S,2S)-2-aminocyclobutane-1-carboxylic acid and cis- and trans-γ-amino-l-proline joined in alternation have been synthesized. High resolution NMR experiments show that peptides containing trans-cyclobutane amino acid residues adopt a more folded structure in solution than those containing a cis-cyclobutane residue, which adopt a strand-like structure. The cis/trans relative configuration of the cyclobutane residue is the origin of the folding pattern of each peptide due to either intra- or inter-residue hydrogen-bonded ring formation, whereas the cis/trans isomerism of the γ-amino-l-proline residue does not have a significantly relevant role on the folding ability of these peptides.

    We also recommend Trading Suppliers and Manufacturers of L-Proline benzyl ester hydrochloride (cas 16652-71-4). Pls Click Website Link as below: cas 16652-71-4 suppliers


    Prev:The first protection-free synthesis of magnetic bifunctional l-proline as a highly active and versatile artificial enzyme: Synthesis of imidazole derivatives
    Next: Chemo-enzymatic approach to d-allo-isoleucine)

About|Contact|Cas|Product Name|Molecular|Country|Encyclopedia

Message|New Cas|MSDS|Service|Advertisement|CAS DataBase|Article Data|Manufacturers | Chemical Catalog

©2008 LookChem.com,License: ICP

NO.:Zhejiang16009103

complaints:service@lookchem.com Desktop View