Human interferon \(\gamma \) (hIFN \(\gamma \) ) is an important pleiotropic cytokine that binds to a specific high-affinity cell-surface receptor complex to mediate its cellular effects. In addition, it is known, that hIFN \(\gamma \) also binds with high affinity to heparin and heparan sulfate and that the binding occurs mainly through the protein’s C-terminus. This interaction affects all physico-chemical properties of the cytokine, including its affinity towards its receptor, which could be exploited as a strategy for the development of potential hIFN \(\gamma \) inhibitors. Here we report our efforts at developing an in silico protocol for deriving optimal heparin/heparan sulfate-derived oligosaccharide sequences in terms of net charge and sulfate distribution, that lead to the most favourable and stable binding to a peptide, encompassing the C-terminus of hIFN \(\gamma \) . The developed computational protocol is tested on the interaction of the cytokine’s C-terminal peptide and a specific octasaccharide sequence.