Interaction of Bovine Serum Albumin and Metallothionein

Abstract

Far UV circular dichroism (CD) and fluorescence spectroscopy were used to investigate the interaction between bovine serum albumin (BSA) and metallothionein (MT). Both spectroscopic probes gave proofs on the interaction of the two proteins. At pH 4.0, 7.0 and 9.0, BSA showed a negative increase in ellipticity at the far-UV range in the presence of MT indicating an increase in α-helical content and a decrease in β-sheet structure. In the presence of MT at pH 4.0 and 9.0, a decrease in fluorescence intensity was observed. Tryptophan fluorescence quenching experiments were also performed using acrylamide and KI as quenchers. Under acidic conditions, a four-fold increase in Stern-Volmer constant (K SV ) was observed for BSA + MT. At neutral and basic conditions, a decrease in K SV values were observed which indicates conformational changes in BSA upon binding MT. These changes are close to the region where the tryptophan residues are located in the protein.

Development and Evaluation of Lyophilized Thiolated-Chitosan Wafers for Buccal Delivery of Protein

“…These results are consistent with the crystal structure of BSA (Quiming et al, 2005). The ratios between the mean residue ellipticity at 208 and 222nm ([θ] 208 /[θ] 222 ) were 1.10, 1.11 and 1.11 for native BSA and BSA released from the annealed and non annealed CSTGA-BSA respectively.…”

Fructose-induced modifications of myoglobin: Change of structure from met (Fe3+) to oxy (Fe2+) form

“…Surface accessibility of tryptophan residues in Mb, Fr-Mb6 and Fr-Mb30 was estimated from the dynamic quenching of the protein fluorescence by using acrylamide as a neutral quencher. The tryptophan fluorescence of the protein (3 M) was quenched by adding increasing concentration of the quencher, from which Lehrer plots [20] and Stern-Volmer plots [21] were constructed to measure the surface accessibility of tryptophan residues of the proteins. For AGE estimation, the fluorescence emission spectra (420-520 nm) of the fractions (3 M) were recorded with excitation at 370 nm [22].…”

“…AGE formation in Mb due to fructation was studied by exciting the separated fructated proteins at 370 nm [21]. As shown in Fig.…”

A Study on the Binding of Loperamide to Human Serum Albumin Using Combination of Computational and Experimental Methods

“…So, the conformation of the complex formed between HSA and LOP has been further studied using CD method. HSA has a high percentage of α-helical structure which indicates characteristic strong double minimum signals at 222 and 208 nm [22] (Figure 3). The intensities of the two double minimum signals reflect the amount of helicity of serum albumin.…”