Amino Acid Chirality and Ferrocene Conformation Guided Self-Assembly and Gelation of Ferrocene–Peptide Conjugates
2015
The self-assembly and gelation behavior of a series of mono- and disubstituted ferrocene (Fc)–peptide conjugates as a function of ferrocene conformation and amino acid chirality are described. The results reveal that ferrocene–peptide conjugates self-assemble into organogels by controlling the conformation of the central ferrocene core, through inter- versus intramolecular hydrogen bonding in the attached peptide chain(s). The chirality controlled assembling studies showed that two monosubstituted Fc conjugates FcCO–LFLFLA-OMe and FcCO–LFLFDA-OMe form gels with nanofibrillar network structures, whereas the other two diastereomers FcCO–DFLFLA-OMe and FcCO–LFDFLA-OMe exclusively produced straight nanorods and non-interconnected small fibers, respectively. This suggests the potential tuning of gelation behavior and nanoscale morphology by altering the chirality of constituted amino acids. The current study confirms the profound effect of diastereomerism and no influence of enantiomers on gelation. Correspondingly, the diastereomeric and enantiomeric Fc[CO-FFA-OMe]2 were constructed for the study of chirality-organized structures.
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