Comparative spectroscopic studies on drug binding characteristics and protein surface hydrophobicity of native and modified forms of bovine serum albumin: possible relevance to change in protein structure/function upon non-enzymatic glycation.

The interaction between serum albumin (SA) and drugs has provided an interesting ground for understanding of drug effects, especially in drug distribution and drug-drug interaction on SA, in the case of multi-drug therapy. Determination of the impact of various factors on drug-protein interaction is especially important upon significant binding of drug to albumin. In the present study, the interaction of two drugs (furosemide and indomethacin) with native and modified albumins were investigated by using various spectroscopic methods.

Chaperone-like activity of heme group against amyloid-like fibril formation by hen egg ovalbumin: possible mechanism of action.

It is well accepted that porphyrins related to heme, are effectively able to act as pharmaceutical. For instance, they were found to interfere with the aggregation of beta-amyloid peptide. In present study, the influence of heme concentration on the amyloid-type aggregation of ovalbumin was investigated.