Multiple ligand interaction of alpha-synuclein produced various forms of protein aggregates in the presence of Abeta25-35, copper, and eosin.
Various protein aggregates of alpha-synuclein developed by way of the common protein self-oligomerization in the presence of Abeta25-35, 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.
Kim
Y S
YS
Department of Pathology, Korea University Ansan Hospital, Gojan-Dong, 425-020, Ansan, South Korea.
Lee
D
D
Lee
E K
EK
Sung
J Y
JY
Chung
K C
KC
Kim
J
J
Paik
S R
SR
D016229:Amyloid beta-Peptides / Q000378:metabolism*; D052160:Benzothiazoles; D002478:Cells, Cultured / Q000187:drug effects / Q000378:metabolism; D003300:Copper / Q000378:metabolism*; D004801:Eosine Yellowish-(YS) / Q000378:metabolism*; D005456:Fluorescent Dyes / Q000737:chemistry* / Q000633:toxicity; D008024:Ligands; D008854:Microscopy, Electron; D009419:Nerve Tissue Proteins / Q000187:drug effects / Q000378:metabolism* / Q000648:ultrastructure; D019636:Neurodegenerative Diseases / Q000378:metabolism* / Q000473:pathology / Q000503:physiopathology; D010446:Peptide Fragments / Q000378:metabolism*; D011108:Polymers / Q000138:chemical synthesis; D017434:Protein Structure, Tertiary / Q000187:drug effects / Q000502:physiology; D051843:Synucleins; D013844:Thiazoles / Q000378:metabolism; D051844:alpha-Synuclein
D016229:Amyloid beta-Peptides; D052160:Benzothiazoles; D005456:Fluorescent Dyes; D008024:Ligands; D009419:Nerve Tissue Proteins; D010446:Peptide Fragments; D011108:Polymers; D051843:Synucleins; D013844:Thiazoles; D051844:alpha-Synuclein; C074636:amyloid beta-protein (25-35); C009462:thioflavin T; D003300:Copper; D004801:Eosine Yellowish-(YS)