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Conformational properties of ferrocene peptides containing exchanged sequence of constituent amino acids

We explored the structural properties of ferrocene peptides II [Y-AA-Fca-OMe ; Y = Boc, Ac ; AA = L-Ala, D-Ala ; Fca = 1'-aminoferrocene-1-carboxylic acid] [1] with an exchanged sequence of constituent amino acids relative to previously described I (Y-Fca-AA-OMe ; Y = Boc, Ac ; AA = L-Ala, D-Ala) [2]. In order to examine their conformational properties, peptides II were subjected to spectroscopic analysis (IR, 1H NMR, CD) and molecular modeling (DFT). The alteration of peptides I into II significantly influenced their conformational properties. Conjugates I were stabilized through interchain hydrogen bonding, whereas inter- and intrachain hydrogen bonds were established in their constitutional isomers II. The replacement of the bulky Boc group with an Ac group did not cause major conformational changes, and the absolute configuration of the alanine chiral centers did not affect the conformational properties.

Ferrocene; peptide; conformational analysis

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