Quantifying L-ascorbic acid-driven inhibitory effect on amyloid fibrillation
- Authors
- Lee, Wonseok; Kim, Insu; Lee, Sang Won; Lee, Hyungbeen; Lee, Gyudo; Kim, Sangsig; Lee, Sang Woo; Yoon, Dae Sung
- Issue Date
- 10월-2016
- Publisher
- SPRINGER
- Keywords
- L-ascorbic acid; beta-lactoglobulin amyloid fibril; inhibition effect; thioflavin T fluorescence assay; atomic force microscopy
- Citation
- MACROMOLECULAR RESEARCH, v.24, no.10, pp.868 - 873
- Indexed
- SCIE
SCOPUS
KCI
- Journal Title
- MACROMOLECULAR RESEARCH
- Volume
- 24
- Number
- 10
- Start Page
- 868
- End Page
- 873
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/87461
- DOI
- 10.1007/s13233-016-4126-1
- ISSN
- 1598-5032
- Abstract
- Ascorbic acid, which is widely used as a therapeutic agent for various disorders (e.g. chronic diseases and cancers), has potential therapeutic roles for neurodegenerative disease such as Huntington's, Parkinson's and Alzheimer's diseases. The ability to impede amyloid fibril formation has a great demand on developing clinical medicine with respect to successfully preventing neurodegenerative diseases. Here, we report that L-ascorbic acid inhibits beta-lactoglobulin amyloid formation in vitro. For quantitative characterization of the inhibitory effect of L-ascorbic acid on fibrillation, we performed high-resolution atomic force microscopy and thioflavin T fluorescence assay. Fourier transform infrared spectra indicated secondary structure differences of fibrils formed with and without ascorbic acid. These results suggest great potential of ascorbic acid for use in the prevention or treatment of amyloidogenic diseases.
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- Appears in
Collections - Graduate School > Department of Biotechnology and Bioinformatics > 1. Journal Articles
- College of Engineering > School of Electrical Engineering > 1. Journal Articles
- Graduate School > Department of Bioengineering > 1. Journal Articles
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