4.2 Article

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

Journal

PROTEIN AND PEPTIDE LETTERS
Volume 24, Issue 12, Pages 1113-1119

Publisher

BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/0929866524666170918120936

Keywords

Amorphous aggregation; amyloid aggregation; hydrophobic interactions; beta-lactoglobulin (beta-LG); resveratrol; transmission electron microscopy (TEM)

Funding

  1. Fundamental Research Funds for the Central Universities [KYZ201321]

Ask authors/readers for more resources

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 beta-lactoglobulin. The results demonstrated resveratrol inhibited the amyloid aggregation and enhanced the amorphous aggregation of beta-lactoglobulin. Objectives: The main objective of this study was to investigate the effects of resveratrol on the amyloid aggregation of beta-lactoglobulin. Methods: beta-lactoglobulin was incubated at pH 2.0 and 70 degrees C. ThT fluorescence, Congo red and transmission electron microscopy were used to monitor the formation of amyloid aggregates. In addition, resveratrol was added into beta-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 beta-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 beta-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 beta-lactoglobulin. Conclusion: Our results indicated that resveratrol could effectively inhibit the formation of amyloid aggregates and enhance the formation of amorphous aggregates of beta-lactoglobulin. Thus, resveratrol could be a potential inhibitor for preventing the formation of amyloid aggregates.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.2
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available