Multi-spectroscopic studies of the interaction of new synthesized platin complex with human carrier protein of serum albumin.

Previous reports have shown that protein-drug interaction helps to improve the pharmacokinetics of the drugs. Human serum albumin (HSA) is one of the basic components of blood plasma and it serves as a storage and carrier protein. In the present study, the interaction of a new synthesized Pt [iso]2 complex (cis - [Pt(NH2-Isopentylamine)2(Isopentylglycine)]NO3) with HSA was studied using the spectroscopic methods of fluorescence and circular dichroic (CD) at two different temperatures of 25 and 37 °C. Analysis of the quenching mechanism via Stern-Volmer curve, determination of HSA binding parameters (0.65 × 104 and 2.27 × 104) and standard Gibbs free energy (-25.8, and 21.77) at 25 and 37 °C, respectively, carried out using fluorescence quenching data. Data analysis showed that the static mechanism has the main role in fluorescence quenching. Also, the number of protein binding sites for complex indicated one binding site at two temperatures of 25 and 37 °C. The secondary structure of protein in the presence of different concentrations of Pt(II) complex did not show any significant alterations. Whereas, thermal stability of the HSA was reduced in the presence of complex. Also, thermal analysis obtained the values of ΔG°25 for HSA and HSA in presence of Pt [Iso]2 20, 13, respectively. According to the above results, we concluded that the new synthesized Pt complex can bind to the blood carrier protein of HSA and change the stability of it which can be considered in the design of new drugs.Communicated by Ramaswamy H. Sarma.

Improvement of efficacy and decrement cytotoxicity of oxaliplatin anticancer drug using bovine serum albumin nanoparticles: synthesis, characterisation and release behaviour.

To sustained release of an anticancer drug, oxaliplatin (OX), a non-toxic and biocompatible nanocarrier based on bovine serum albumin (BSA) were synthesised by desolvation method and characterised using Fourier-transform infrared (FTIR) spectroscopy, field emission scanning electron microscopy (FESEM), atomic force microscopy (AFM) and dynamic light scattering. The results showed that the BSA nanoparticles (BSANPs) with a mean magnitude of 187.9 ± 1.2 nm have spherical morphology with a smooth surface and a uniform distribution. Furthermore, OX was loaded onto the BSANPs and the loading was confirmed by FTIR, AFM and FESEM techniques. The percentage of encapsulation efficiency and drug loading were determined by absorption spectroscopy (UV-vis). The drug release studies showed that release of OX from BSANPs exhibited slower release rate. However, the release kinetics followed the first-order kinetic for both of them with the non-Fickian release behaviour. The electrochemical analysis showed stability of OX loaded onto the BSANPs (OX@BSANPs) and confirmed the diffusion mechanism. Furthermore, the results of MTT assay revealed increasing of normal cell viability and cancer cell death in the OX@BSANPs compared to only OX. It was shown that the BSANPs could be safely used as a biocompatible nanocarrier for the sustained release of OX.