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Additional file 1. Supplementary figures describe the schematic of Fe-based NWs oxidation and its evaluation, the variation of the relaxation rates as a function of the Fe-based NW concentration at 1.5 T for different NW formulations, the decay of the r2 values obtained at 7 T across the time for different NW formulations, the influence of the NWs’ magnetization in the r2 decay across time, and four axial consecutive slices of 200 µm of thickness across the brain of a mouse implanted with BSA-NWs labeled cells. Supplementary tables describe the determination of the oxidation level of Fe NWs through elemental quantification, and the longitudinal (r1), transversal (r2) relaxivities and r2/r1 ratio of different nanowire formulations at 1.5 T. Supplementary methods describe the synthesis of nanowires, the magnetic characterization of nanowires, the quantification of iron nanowires, the relaxivity measurements at 1.5 T, the magnetization effect of iron nanowires at the 7 T, the preparation of cell suspensions for in vitro MRI detection and the preparation of agar gels for MRI imaging phantom studies.

Resumen del póster presentado al XL Congreso de la Sociedad Española de Bioquímica y Biología Molecular (SEBBM), celebrado en Barcelona del 23 al 26 de octubre de 2017., Myocardial fibroblast activation coupled with extracellular matrix production is a pathological signature of myocardial fibrosis and is governed by the transforming growth factor TGFβ-Smad2/3 signaling. Targeting TGFβ itself to reduce pathological fibrosis carries cellular homeostasis deregulation with adverse consequences. We sought to determine the anti-fibrotic eff ects of 90 kDa heat shock protein (Hsp90) downregulation, a chaperone that associates to the TGFβ cascade in this process. To this end, we utilize a new biotechnological Hsp90 inhibitor CTPR390-488 with specific Hsp90 ligand binding properties that maintain its chaperon activity and a fl uorophore attached to be tracked. Gene and protein detections indicated that CTPR390-488 inhibited collagen synthesis, ultrastructural analysis indicated that collagen deposition was diminished and cell tracking assays showed a decrease in cell motility, similarly to fi broblasts from Hsp90aa1 knock out mouse. The anti-fi brotic effects of CTPR390-488 were associated with TGFβ receptor I–Hsp90 complex disruption through in silico studies and phosphorylation assays indicated inhibition of Smad2/3 activation. Reduction of the extracellular matrix through Hsp90aa1 downregulation or CTPR390-488 action decreased fibroblasts motility and diminished the extent of myocardial fibrosis in the Ang II fibrotic mouse model. An insight into the role of CTPR390-488 as a therapeutic biomarker was proved with plasma measurements indicating increasing concentrations of the biomolecule in the mice subjected to Ang II infusion. In conclusion, this is the first study to demonstrate that a fl uorescent CTPR390-488 blocks collagen expression and motility of myocardial TGFβ-activated fi broblasts and ameliorates angiotensin II-induced myocardial fibrosis in vivo.