Studies on the interactions between human serum albumin and imidazolium [trans-tetrachlorobis(imidazol)ruthenate(III)]

New advances in the study on the interaction of [Cr(phen)2(dppz)]3+ complex with biological models; association to transporting proteins

“…However, the CD spectra of serum albumins in the presence and absence of Cr(III) complex are similar in shape, indicating that the structure of BSA and HSA is also predominantly α-helical. From the above results, it is apparent that the effect of [Cr(phen) 2 (dppz)] 3+ on serum albumins causes a conformational change in the proteins, with loss of helical stability as found for ruthenium(III)-imidazole complex [33]. Furthermore, the α-helical contents of serum albumins in the presence and absence of Cr(III) complex were calculated by quantitative analysis of the CD spectra data, using Eq.…”

Synthesis and crystal structure determination of copper(II)-complex: In vitro DNA and HSA binding, pBR322 plasmid cleavage, cell imaging and cytotoxic studies

“…The fluorescence quenching of HSA at different temperatures (299, 308 and 318 K) were determined using the SterneVolmer equation (Eq. (1)) [47]:…”

Investigation of interaction between human serum albumin and N6‐(2‐hydroxyethyl)‐adenosine by fluorescence spectroscopy and molecular modelling

“…Simultaneously, a blue-shift of the maximum emission wavelength occurred. These factors indicate that an interaction occurred between HSA and HEA and that the microenvironment around the Trp-214 residue was changed after the addition of HEA (20). Figure 3 shows the UV absorption spectra of the systems in the presence and absence of HEA.…”