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Our findings revealed that the enzyme remained stable across all crowding agents tested, and at a concentration of 30 mg/ml of the crowders, we observed an enhancement in vaPPO activity, indicating the enzymes resilience and suitability for biotechnological applications that occur in the presence of other biomolecules and contaminants (Fig

Dihexa binds with high affinity to HGF and both dihexa and its parent compound Norleucine 1-AngIV induce c-Met phosphorylation in the presence of subthreshold concentrations of HGF and augment HGF-dependent cell scattering