Anti-aggregation properties of trehalose on heat-induced secondary structure and conformation changes of bovine serum albumin.

During our experimental work, aggregation of bovine serum albumin was obtained incubating the protein solution at 60 degrees C to investigate temperature-induced secondary structure, conformation changes and anti-aggregative activity of trehalose. IR-measurements suggested that in the presence of 1.0M of trehalose there is a little increase in short segment connecting alpha-helical and a clearly decrease in the loss of alpha-helix structure and in the formation of intermolecular and antiparellel beta-sheet up to 78 and 55%, respectively. Useful information also arose following the temperature evolution of Amide I' band profile in the range of temperature between 25 and 90 degrees C in absence or in presence of 1.0M trehalose. Complementary information is obtained by electrophoresis, circular dichroism, fluorescence spectroscopy, titration of SH groups and light scattering measurements. Results encouraged biotechnology and pharmaceutical application of the disaccharide and provided evidence for its utilization in degenerative diseases evolving via aggregation process. Copyright (c) 2010 Elsevier B.V. All rights reserved.