海藻糖对热诱导牛血清白蛋白二级结构和构象变化的抗聚集性质。

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

机构信息

Department of Organic and Biological Chemistry, University of Messina, Salita Sperone 31, Villaggio S. Agata, Messina, Italy.

出版信息

Biophys Chem. 2010 Apr;147(3):146-52. doi: 10.1016/j.bpc.2010.01.010. Epub 2010 Feb 1.

DOI:10.1016/j.bpc.2010.01.010

PMID:20171005

Abstract

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.

摘要

在我们的实验工作中，通过在 60°C 下孵育蛋白质溶液来获得牛血清白蛋白的聚集，以研究海藻糖对温度诱导的二级结构、构象变化和抗聚集活性的影响。IR 测量表明，在 1.0M 海藻糖存在下，短连接α-螺旋的片段略有增加，α-螺旋结构的损失明显减少，分子间和反平行β-折叠的形成分别增加了 78%和 55%。在 25 至 90°C 的温度范围内，在没有或存在 1.0M 海藻糖的情况下，酰胺 I'带谱的温度演化也产生了有用的信息。电泳、圆二色性、荧光光谱、SH 基团滴定和光散射测量提供了补充信息。这些结果鼓励了海藻糖在生物技术和制药领域的应用，并为其在通过聚集过程演变的退行性疾病中的应用提供了证据。