Epitope Mapping Immunoassay Analysis of the Interaction between -Amyloid and Fibrinogen
- Authors
- Giau, Vo Van; An, Seong Soo A.
- Issue Date
- 1-Feb-2019
- Publisher
- MDPI
- Keywords
- Alzheimer' s disease; amyloid-; epitope mapping; ligand; fibrinogen
- Citation
- INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, v.20, no.3
- Journal Title
- INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
- Volume
- 20
- Number
- 3
- URI
- https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/1862
- DOI
- 10.3390/ijms20030496
- ISSN
- 1422-0067
- Abstract
- The vast majority of patients with Alzheimer's disease (AD) suffer from impaired cerebral circulation. Substantial evidence indicates that fibrinogen (Fbg) and fibrin clot formation play an important role in this circulatory dysfunction in AD. Fbg interacts with -amyloid (1-42) (A), forming plasmin-resistant abnormal blood clots, and increased fibrin deposition has been discovered in the brains of AD patients and mouse models. In this study, biochemical approaches and the epitope mapping immunoassay were employed to characterize binding epitopes within the Fbg and complementary epitopes in A. We discovered the A5-25 peptide as the most critical region for the interaction, which can be inhibited by specific monoclonal and polyclonal antibodies against the central region of A. A binding to Fbg may block plasmin-mediated fibrin cleavage at this site, resulting in the generation of increased levels of plasmin-resistant fibrin degradation fragments. Our study elucidates the A-Fbg interaction that may involve the mechanism by which A-Fbg binding delays fibrinolysis by plasmin, providing valuable information in the development of therapeutic approaches for AD.
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Collections - 바이오나노대학 > 바이오나노학과 > 1. Journal Articles
- 산업·환경대학원 > 산업환경공학과 > 1. Journal Articles
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