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Multiple ligand interaction of α-synuclein produced various forms of protein aggregates in the presence of Aβ25-35, copper, and eosin

Authors
 Young-Sik Kim  ;  Daekyun Lee  ;  Eun-Kyung Lee  ;  Jee Young Sung  ;  Kwang Chul Chung  ;  Jongsun Kim  ;  Seung R Paik 
Citation
 BRAIN RESEARCH, Vol.908(1) : 93-98, 2001 
Journal Title
 BRAIN RESEARCH 
ISSN
 0006-8993 
Issue Date
2001
MeSH
Amyloid beta-Peptides/metabolism* ; Cells, Cultured/drug effects ; Cells, Cultured/metabolism ; Copper/metabolism* ; Eosine Yellowish-(YS)/metabolism* ; Fluorescent Dyes/chemistry* ; Fluorescent Dyes/toxicity ; Ligands ; Microscopy, Electron ; Nerve Tissue Proteins/drug effects ; Nerve Tissue Proteins/metabolism* ; Nerve Tissue Proteins/ultrastructure ; Neurodegenerative Diseases/metabolism* ; Neurodegenerative Diseases/pathology ; Neurodegenerative Diseases/physiopathology ; Peptide Fragments/metabolism* ; Polymers/chemical synthesis ; Protein Structure, Tertiary/drug effects ; Protein Structure, Tertiary/physiology ; Synucleins ; Thiazoles/metabolism ; alpha-Synuclein
Keywords
α-Synuclein ; Self-oligomerization ; Protein aggregation ; Cytotoxicity ; Parkinson’s disease
Abstract
Various protein aggregates of α-synuclein developed by way of the common protein self-oligomerization in the presence of Aβ25-35, copper, and eosin were examined. All the aggregates exhibited congo red birefringence although the actual amounts of the aggregates were varied as determined by thioflavin T binding fluorescence. When their morphologies were analyzed in relation to in vitro cytotoxicity, the smallest granular aggregates obtained with copper exhibited the highest cytotoxicity, while the fibrous structures by eosin did not affect the cell.
Full Text
http://www.sciencedirect.com/science/article/pii/S0006899301025756
DOI
10.1016/S0006-8993(01)02575-6
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Microbiology (미생물학교실) > 1. Journal Papers
Yonsei Authors
Kim, Jong Sun(김종선) ORCID logo https://orcid.org/0000-0002-3149-669X
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/142563
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