Journal of the Korean Magnetic Resonance Society (한국자기공명학회논문지)
- Volume 8 Issue 1
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- Pages.19-27
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- 2004
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- 1226-6531(pISSN)
Structure of CT16 in the C-terminal of Amyloid Precursor Protein Studied by NMR Spectroscopy
- Lee, Kyoung-Ik (Department of Chemistry, Konkuk University) ;
- Baek, Dong-Ha (Department of Chemistry, Konkuk University) ;
- Shin, Song-Yub (Department of Bio-Materials, Graduate School and Research Center for Proteineous Materials, Chosun University) ;
- Kim, Yang-Mee (Department of Chemistry, Konkuk University)
- Published : 2004.06.01
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
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