Cardona Mejías, Aracelis

Publication Search Results

Now showing 1 - 1 of 1

Characterization of Ti(IV) - transferring binding interactions
(2006) Cardona Mejías, Aracelis; Meléndez, Enrique; College of Arts and Sciencies - Sciences; Cádiz, Mayra E.; Vera, Marisol; Department of Chemistry; Maldonado, Sandra L.
Human transferrin (Tr) is a 80kDa protein that firmly binds iron at two specific binding sites. It has been implicated in the transport and delivery of metal that have anticancer properties. This research study the interaction between Tr and Cp₂TiCl₂ and [Cp₂Ti(L-Cys)₂]Cl₂, [Cp₂Ti(L-Met)₂]Cl₂ and [Cp₂Ti(D-Pen)₂]Cl₂ complexes, in order to pinpoint the influence of aminoacids on the binding affinity of Ti⁽ᴵⱽ⁾ to transferrin. Nuclear magnetic resonance experiments of the interactions showed new signals due to changes in protein glycan chains. This suggests that Ti⁽ᴵⱽ⁾ is being loaded into the iron binding sites. Experiments of 2D NMR support these findings. Ultraviolet titrations of the protein with Ti complexes exhibited an increase in 242/295nm bands and the appearance of the 321nm band. Interactions of Cp₂MoCl₂ and Cp₂VCl₂ with Tr were also studied by UV-Vis. Simultaneous quantification of Ti and S by ICP-AES was used to calculate the Ti/protein mole ratio. Since Ti₂-Tr interactions have been characterized for the new titanocene-aminoacid complexes, their development as anticancer drugs can be proposed.