Impact of low- and high-molecular-mass components of human serum on NAMI-A binding to transferrin
| LEADER | caa a22 4500 | ||
|---|---|---|---|
| 001 | 605507414 | ||
| 003 | CHVBK | ||
| 005 | 20210128100632.0 | ||
| 007 | cr unu---uuuuu | ||
| 008 | 210128e20150601xx s 000 0 eng | ||
| 024 | 7 | 0 | |a 10.1007/s00775-015-1255-5 |2 doi |
| 035 | |a (NATIONALLICENCE)springer-10.1007/s00775-015-1255-5 | ||
| 245 | 0 | 0 | |a Impact of low- and high-molecular-mass components of human serum on NAMI-A binding to transferrin |h [Elektronische Daten] |c [K. Śpiewak, M. Brindell] |
| 520 | 3 | |a 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 to its preferential binding to transferrin receptor. Here, we showed that holotransferrin is able to bind NAMI-A as readily as apotransferrin. The simulation of biological conditions of human serum performed by application of simplified serum models allowed to analyse ruthenium distribution between transferrin and albumin. The presence of physiological concentration of albumin (ca. 18-fold excess over Tf) resulted in a twofold decrease of ruthenium binding to Tf. Interestingly, the introducing of low-molecular-mass components of serum dramatically increased the ruthenation of Tf. Intermolecular competition binding studies between transferrin and albumin showed that both proteins bound similar amount of ruthenium species. Investigation of NAMI-A binding to Tf in human serum showed that this protein was not the major binding partner for Ru complex. However, in spite of many competing proteins still the ruthenation of Tf was observed. The lack of free Ru species (protein unbounded) after incubation with human serum allowed to make an assumption of high affinity of NAMI-A towards serum proteins. | |
| 540 | |a The Author(s), 2015 | ||
| 690 | 7 | |a Transferrin |2 nationallicence | |
| 690 | 7 | |a Albumin |2 nationallicence | |
| 690 | 7 | |a Serum |2 nationallicence | |
| 690 | 7 | |a NAMI-A |2 nationallicence | |
| 690 | 7 | |a FPLC |2 nationallicence | |
| 700 | 1 | |a Śpiewak |D K. |u Department of Inorganic Chemistry, Faculty of Chemistry, Jagiellonian University, Ingardena 3, 30-060, Kraków, Poland |4 aut | |
| 700 | 1 | |a Brindell |D M. |u Department of Inorganic Chemistry, Faculty of Chemistry, Jagiellonian University, Ingardena 3, 30-060, Kraków, Poland |4 aut | |
| 773 | 0 | |t JBIC Journal of Biological Inorganic Chemistry |d Springer Berlin Heidelberg |g 20/4(2015-06-01), 695-703 |x 0949-8257 |q 20:4<695 |1 2015 |2 20 |o 775 | |
| 856 | 4 | 0 | |u https://doi.org/10.1007/s00775-015-1255-5 |q text/html |z Onlinezugriff via DOI |
| 898 | |a BK010053 |b XK010053 |c XK010000 | ||
| 900 | 7 | |a Metadata rights reserved |b Springer special CC-BY-NC licence |2 nationallicence | |
| 908 | |D 1 |a research-article |2 jats | ||
| 949 | |B NATIONALLICENCE |F NATIONALLICENCE |b NL-springer | ||
| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1007/s00775-015-1255-5 |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Śpiewak |D K. |u Department of Inorganic Chemistry, Faculty of Chemistry, Jagiellonian University, Ingardena 3, 30-060, Kraków, Poland |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Brindell |D M. |u Department of Inorganic Chemistry, Faculty of Chemistry, Jagiellonian University, Ingardena 3, 30-060, Kraków, Poland |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t JBIC Journal of Biological Inorganic Chemistry |d Springer Berlin Heidelberg |g 20/4(2015-06-01), 695-703 |x 0949-8257 |q 20:4<695 |1 2015 |2 20 |o 775 | ||