Bovine serum albumin

About: Bovine serum albumin is a research topic. Over the lifetime, 19981 publications have been published within this topic receiving 571291 citations. The topic is also known as: BSA.

Exploring hydrophobic subdomain IIA of the protein bovine serum albumin in the native, intermediate, unfolded, and refolded states by a small fluorescence molecular reporter

Abstract: A simple intramolecular charge transfer (ICT) compound, 5-(4-dimethylamino-phenyl)-penta-2,4-dienoic acid methyl ester (DPDAME), has been documented to be a potential molecular reporter for probing microheterogeneous environments of a model transport protein bovine serum albumin (BSA) using spectroscopic techniques. Meteoric modifications to the emission profile of DPDAME upon addition of BSA come out to be a result of its binding to hydrophobic subdomain IIA. The highly polarity-sensitive ICT emission of DPDAME is found to be a proficient extrinsic molecular reporter for efficient mapping of native, intermediate, unfolded, and refolded states of the protein. Experimental data coupled with a reinforcing support from theoretical simulation using CHARMM22 software confirm the binding site of the probe to be the subdomain IIA of BSA, while FRET study reveals a remarkably close approach of our extrinsic molecular reporter to Trp-212 (in domain IIA): the distance between DPDAME and Trp-212 is 1.437 nm. The caliber of DPDAME as an external fluorescence marker also extends to the depiction of protein-surfactant (BSA-SDS) interaction to commendable fruition. Additionally, the protective action of small amounts of SDS on urea-denatured protein is documented by polarity-sensitive ICT emission of the probe. The present study also reflects the enhancement of the stability of BSA with respect to chemically induced denaturation by urea as a result of binding to the probe DPDAME.

The conformational structure of bovine serum albumin layers adsorbed at the silica-water interface

Abstract: The adsorption of bovine serum albumin (BSA) at the hydrophilic silica−water interface has been studied using specular neutron reflection. The measurements were made over the concentration range from 0.005 to 0.5 g dm-3. The surface excess was found to vary from 1.8 to 2.4 mg m-2. The layers could be modeled using a single uniform layer model, suggesting that over the concentration range studied there is insignificant denaturation, which would lead to a more fragmented peptide distribution and hence layers of different density. Comparison of the layer thickness with the dimensions of the ellipsoidal structure of the globular solution structure indicates that the molecules adsorb sideways-on. Nevertheless, the layer thickness is always less than 40 A, suggesting that adsorption onto the hydrophilic surface results in some structural deformation. The increase of layer thickness with bulk concentration suggests that the extent of the distortion is reduced as the lateral repulsion between protein molecules in...