41a, 42a). Here, the BSA-ligand interactions protected the molecules with higher hydrophobic properties, particularly H-Tyra. This was followed by H-Styr, then H-Tyros against the oxidative effects of H2O2 (supplementary figs. ), compared to the BSA-free system (supplementary figs. ). In addition, considering the functionality of phenol to donate electron density via the resonance effect, the peroxidative catalytic functions of hemin and H-Tyros, complexed to BSA were enhanced on the treatment with H2O2 and phenol. However, in the BSA-free system, the effects of hemin were absent, while H-Tyros showed a significant peroxidative effect for the decomposition of the oxidizing agent. This can be explained by the reported roles of tyrosine in electron transfer due to its redox activity and its electron donating ability . Although this should be the case with H-Tyra as well, its relatively high affinity towards the BSA seems to affect its functionality, with a possible reversal of phenol effects. Similarly, in the case with H-Styr, it showsed the highest affinity towards BSA, H2O2 enhanced its oxidation, with no protecting effects of phenol. This may relate to the more stable conjugated system within the H-Styr structure in which the iron ion is more prone to oxidation. This supports our previous hypothesis that H-Styr is most probably having a Fe(II) character, which in turn will be more prone to oxidation These studies were followed by evaluating the effects of • NO-scavenging on cell migration via both transwell cell migration and wound healing assay. In the former assay, the tested cells generally migrate towards the lower side of the migration membrane under the effect of a certain chemoattractant.