engleski

Synthesis, conformational analysis and preliminary biological evaluation of conjugates of ferrocene and hydrophobic amino acids

Conjugates of different ferrocene scaffolds and amino acids are recognized as peptidomimetics because they are able to adopt different elements of peptide secondary structure (turns, coils, sheets) based on intramolecular hydrogen bonding. [1-3] Peptide sequences rich in hydrophobic amino acids have desirable properties (high solubility, stability and bioavailability) that allow them to enhance the biological activity of the corresponding peptidomimetics. [4] To investigate the influence of the chirality of the hydrophobic amino acid and protecting groups (Ac or Boc) on the conformational properties and biological activity, we prepared ferrocene dipeptides Ac (Boc)L(D)AANHFnCOOMe (I) [Fn=ferrocenylene, AA= valine, leucine or phenylalanine, (Figure 1)] by the standard HOBt/EDC method. Dipeptides I are subjected to detailed spectroscopic analysis (IR, NMR and CD) in order to determine their conformational properties. Their preliminary biological evaluation is carried out by measuring the antimicrobial and antioxidant activity (DPPH and FRAP methods).

ferrocene ; peptidommimetics ; hydrophobic amino acids ; conformational anlysis ; biological evaluation

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