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Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 26, Number 8
BKCSDE 26(8)
August 20, 2005 

Structure of CT26 in the C-terminal of Amyloid Precursor Protein Studied by NMR Spectroscopy
Dong-Il Kang, Dongha Baek, Song Yub Shin, Yangmee Kim*
Alzheimer’s disease, APP, CT26, NMR spectroscopy, CD spectroscopy
C-terminal fragments of APP (APP-CTs), that contain Aβ sequence, are found in neurotic plaques, neurofibrillary tangles and the cytosol of lymphoblastoid cells obtained from AD patients. CT26, Thr639- Asp664 (TVIVITLVMLKKKQYTSIHH GVVEVD) includes not only the transmembrane domain but also the cytoplasmic domain of APP. This sequence is produced from cleavage of APP by caspase and γ-secretase. In this study, the solution structure of CT26 was investigated using NMR spectroscopy and circular dichroism (CD) spectropolarimeter in various membrane-mimicking environments. According to CD spectra and the tertiary structure of CT26 determined in TFE-containing aqueous solution, CT26 has an α-helical structure from Val2 to Lys11 in TFE-containing aqueous solution. However, according to CD data, CT26 adopts a β-sheet structure in the SDS micelles and DPC micelles. This result implies that CT26 may have a conformational transition between α-helix and β-sheet structure. This study may provide an insight into the conformational basis of the pathological activity of the C-terminal fragments of APP in the model membrane.
1225 - 1228
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