Impact of low- and high-molecular-mass components of human serum on NAMI-A binding to transferrin

摘要: Imidazolium trans-tetrachloridodimethylsulfoxideimidazolruthenate(III), NAMI-A, a novel antimetastatic ruthenium complex was investigated towards affinity to transferrin (Tf), whether Tf-Ru adducts might be formed after its intravenous injection. Studies were focused on the holotransferrin due preferential binding receptor. Here, we showed that is able bind NAMI-A as readily apotransferrin. The simulation of biological conditions human serum performed by application simplified models allowed analyse distribution between and albumin. presence physiological concentration albumin (ca. 18-fold excess over Tf) resulted in twofold decrease Tf. Interestingly, introducing low-molecular-mass components dramatically increased ruthenation Intermolecular competition studies both proteins bound similar amount species. Investigation Tf this protein not major partner for Ru complex. However, spite many competing still observed. lack free species (protein unbounded) incubation with make an assumption high proteins.