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Structure of CT16 in the C-terminal of Amyloid Precursor Protein Studied by NMR Spectroscopy

김양미|이견직|백동하|신송엽
한국자기공명학회 (Korean Magnetic Resonance Society)|2004.06|Journal of the Korean Magnetic Resonance Society|제8권 제1호|pp. 19-27

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Abstract

C-terminal fragments of APP (APP-CTs), that contain complete Abeta sequence, are found in neuritic plaques, neurofibrillary tangles and the cytosol of lymphoblastoid cells obtained from AD patients. CT16, Lys649-Asp664 (KKQYTSIHHGVVEVD) has been known as the most toxic part in the C-terminal fragment of amyloid precursor protein (APP). The solution structure of CT16 was investigated using NMR spectroscopy in various membrane-mimicking environments. According to Circular Dichroim (CD) spectra, CT16 has a random structure in aqueous solution, while conformational change was induced by addition of TFE and SDS micelle. Tertiary structure as determined by NMR spectroscopy shows that CT16 has a β-turn conformation in trifluoroethanol-containing aqueous solution

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