Cystine bridges play a crucial role in protein folding, allosteric control and maintenance of biological activity. For this reason replacement of cystine bridges with synthetic isosteres, such as with dicarba bridges, provide exciting opportunities to explore the structural, chemical and pharmacokinetic properties of the peptide. Olefin metathesis provides an expedient route to form unsaturated dicarba bridges within the peptide that have structural resemblance to native cystine. Interestingly, significant differences in biological activity can often be observed between the E- and Z- dicarba peptide isomers, important not only for their pharmaceutical potential but also insights into structural role of disulfide bridge in the native peptide. However, traditional olefin metathesis catalysts provide mixtures of both the E- and Z- isomers in a ratio that is highly sequence dependent. In the absence of a regioselective olefin metathesis catalyst applicable to the synthesis of dicarba peptides, a simple method for determining the geometry of the resultant unsaturated diaminosuberic acid bridge is crucial. Although numerous spectroscopic and crystallographic techniques have been employed, their success is often highly sequence dependent. Hence, a reliable technique for determination of olefin geometry in unsaturated diaminosuberic acid bridges is of high interest. In this context, we aim to investigate a synthetic and spectroscopic approach as two independent methods to unambiguously elucidate alkene geometry in Δ4,5-aminosuberic acid derived peptides.