The interaction of bovine serum with leucomalachite green (LMG) was investigated by spectroscopic methods . LMG was found to quench the intrinsic fluorescence of BSA by dynamic quenching. High quenching constant suggested that LMG can form a complex with BSA. Binding constant and number of binding site were determined. The thermodynamic parameters suggested the main interacting force is hydrophobic forces . The effect of LMG on the conformation of BSA was analyzed by synchronous fluorescence spectroscopy . RLS spectra were also used to reconfirm the formation of complex between BSA and LMG.
In this study, phosphate glasses embedded with Fe 2 O 3 quantum dots were prepared via a conventional melt quenching technology with further heat treatment. The effect of Fe 2 O 3 content on the structural, optical and magneto-optical properties was investigated. The results showed that the addition of Fe 2 O 3 had no obvious influence on the structure units that built up the host glass and the amorphous nature of glass. In the glass matrix , the existence of Fe 2 O 3 quantum dots was confirmed by high resolution transmission electron microscope . Meanwhile, optical study clearly demonstrated a red shift in optical cut-off wavelength resulted from the size quantization effect. The highest Verdet constant (22.33°/T-cm) was measured for the glass containing 1 mol% Fe 2 O 3 , which was ~ 7 times higher than that of the glass matrix. As the increment of Fe 2 O 3 contents, a phase evolution of Fe 2 O 3 quantum dots from amorphous phase to γ-Fe 2 O 3 phase was recorded due to the Ostwald Ripening effect. Interestingly, a concentration quenching phenomenon in Verdet constant was observed along with the phase evolution of Fe 2 O 3 quantum dots. When the content of Fe 2 O 3 is up to 2 mol%, the glass exhibited paramagnetism with the Verdet constant of − 2.833°/T-cm. This finding can provide a new idea for the development of quantum dot embedded magneto-optical glass.
Butachlor is an effective herbicide to deal with undesired weeds selectively and is used at high levels in Asian countries. However, its interaction and impairment effect on BSA was still not clear. In this study, we investigated the interaction between butachlor and bovine serum albumin (BSA) by multi-spectroscopic methods including UV absorption , circular dichroism (CD) spectra, Fourier transform infrared (FTIR) spectra and fluorescence spectra under physiological conditions (pH = 7.4). The results revealed that there was a static quenching of BSA induced by butachlor stemmed from the formation of complex. Based on thermodynamic data, the interaction of butachlor with BSA was due to happen, and van der Waals force as well as hydrogen bond were the major forces contributed to the interaction. The binding constant K b and number of binding site of butachlor with BSA were 5.158 × 10 5 and 1.372 at 303 K, respectively. The distance r between donor (BSA) and acceptor (butachlor) was 0.113 nm, obtained according to the Förster theory. The results revealed that butachlor induced conformational changes in BSA but the secondary structure of BSA was still retained. In addition, the microenvironment around chromophore residues of BSA, for example, tryptophan , changed as well, resulting from the formation of more hydrogen bonds.
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