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 ${\beta}$-turn conformation in trifluoroethanol-containing aqueous solution.

Keywords