白藜芦醇诱导β-乳球蛋白从淀粉样聚集转变为无定形聚集

Resveratrol Induces the Conversion from Amyloid to Amorphous Aggregation of β-lactoglobulin>.

作者信息

Ma Baoliang, Zhang Fan, Liu Yujie, Xie Jinbing, Wang Xiaofei

机构信息

Department of Physics, Science of College, Nanjing Agricultural University, Nanjing 210095, China.

College of Engineering and Applied Sciences, Nanjing University, Nanjing 210093, China.

出版信息

Protein Pept Lett. 2018 Feb 8;24(12):1113-1119. doi: 10.2174/0929866524666170918120936.

DOI:10.2174/0929866524666170918120936

PMID:28925863

Abstract

BACKGROUND

Protein aggregation is a wide-ranging phenomenon. Protein aggregation mainly includes two types: one is amorphous aggregation, the other is amyloid aggregation. In particular, amyloid aggregation in vivo can cause several fatal diseases. We have investigated the influence of resveratrol on the amyloid aggregation of β-lactoglobulin. The results demonstrated resveratrol inhibited the amyloid aggregation and enhanced the amorphous aggregation of β- lactoglobulin.

OBJECTIVES

The main objective of this study was to investigate the effects of resveratrol on the amyloid aggregation of β-lactoglobulin.

METHODS

β-lactoglobulin was incubated at pH 2.0 and 70 °C. ThT fluorescence, Congo red and transmission electron microscopy were used to monitor the formation of amyloid aggregates. In addition, resveratrol was added intoβ-lactoglobulin solutions. Intrinsic fluorescence, Circular dichroism and 1-Anilinonaphthalene-8-sulfonic Acid (ANS) fluorescence were used to investigate conformational and hydrophobic changes. Furthermore, we also studied the effect of resveratrol on the amyloid aggregation of β-lactoglobulin by using ThT fluorescence, Congo red and transmission electron microscopy at acidic pH and high temperature.

RESULTS

ThT fluorescence, Congo red and transmission electron microscopy analysis showed that β-lactoglobulin could form the amyloid fibrils when it was incubated under acidic pH and high temperature conditions. At the same time, the analysis also demonstrated resveratrol inhibited the formation of amyloid aggregates and enhanced the formation amorphous aggregates. Intrinsic fluorescence, Circular dichroism and 1-Anilinonaphthalene-8-sulfonic Acid (ANS) fluorescence analysis indicated that resveratrol could alter the conformation and increased the hydrophobicity of β- lactoglobulin.

CONCLUSION

Our results indicated that resveratrol could effectively inhibit the formation of amyloid aggregates and enhance the formation of amorphous aggregates of β-lactoglobulin. Thus, resveratrol could be a potential inhibitor for preventing the formation of amyloid aggregates.

摘要

背景

蛋白质聚集是一种广泛存在的现象。蛋白质聚集主要包括两种类型：一种是无定形聚集，另一种是淀粉样聚集。特别是，体内的淀粉样聚集会引发多种致命疾病。我们研究了白藜芦醇对β-乳球蛋白淀粉样聚集的影响。结果表明，白藜芦醇抑制了β-乳球蛋白的淀粉样聚集，并增强了其无定形聚集。

目的

本研究的主要目的是探究白藜芦醇对β-乳球蛋白淀粉样聚集的影响。

方法

将β-乳球蛋白在pH 2.0和70°C条件下孵育。使用硫黄素T荧光、刚果红和透射电子显微镜监测淀粉样聚集体的形成。此外，将白藜芦醇添加到β-乳球蛋白溶液中。利用内源荧光、圆二色性和1-苯胺基萘-8-磺酸（ANS）荧光研究构象和疏水变化。此外，我们还通过在酸性pH和高温条件下使用硫黄素T荧光、刚果红和透射电子显微镜研究了白藜芦醇对β-乳球蛋白淀粉样聚集的影响。