The design of peptide mimetic compounds is greatly facilitated by the identification of functionalities that call act as peptide replacements. The fluoroalkene moiety has recently been employed for that purpose. The purpose of this work is to examine the conformational ramifications of replacing peptide bonds with fluoroalkene moieties, thus generating peptidomimetics. the alanine dipeptide analogue (ADA) was chosen as a model compound. Three peptidomimetic systems were investigated including one generated by replacement of both peptide bonds of ADA, designated as DFA, and those generated by the single replacement of the C-terminal peptide bond and N-terminal peptide bond, designated as CFA and NFA, respectively. Conformations for all three systems were generated by exhaustive Monte Carlo searching. Relative conformational energies were calculated at the MP2/aug-cc-pVTZ/MP2/aug-cc-pVDZ (for DFA), MP2/-aug-cc-pVTZ/MP2/6-311+G(d,p), B3LYP/6-31+G(d)//B3LYP/6-31+G(d), and MMFF levels of theory. Aqueous phase conformational preferences were determined through calculations making use of continuum hydration models. The results indicate that replacement of both peptide bonds of ADA generates a peptidomimetic with conformational preferences where extended conformations are favored and the conformational profile is relatively insensitive to the nature of the Surrounding medium. This is in contrast to ADA where the conformational preferences depend highly on the surrounding medium and where folded conformations with intramolecular hydrogen bonds are important in the absence of all interacting solvent. CFA and NFA are found to exhibit conformational preferences that do in some ways more closely resemble those of the alanine dipeptide analogue. This is particularly true ill the ease of NFA where interactions between the NH and CF groups are reminiscent of the intramolecular hydrogen bonding possible in ADA.