Interaction of Thioflavin T with amyloid fibrils of apolipoprotein A-I N-terminal fragment Resonance energy transfer study》.pdfVIP

Journal of Structural Biology 185 (2014) 116–124 Contents lists available at ScienceDirect Journal of Structural Biology journal homepage: /locate/yjsbi Interaction of Thioflavin T with amyloid fibrils of apolipoprotein A-I N-terminal fragment: Resonance energy transfer study Mykhailo Girych a,⇑, Galyna Gorbenko a, Valeriya Trusova a, Emi Adachi b, Chiharu Mizuguchi b, Kohjiro Nagao b, Hiroyuki Kawashima c, Kenichi Akaji c, Sissel Lund-Katz d, Michael C. Phillips d, Hiroyuki Saito b a Department of Nuclear and Medical Physics, V.N. Karazin Kharkiv National University, 4 Svobody Sq., Kharkov 61077, Ukraine b Institute of Health Biosciences, Graduate School of Pharmaceutical Sciences, The University of Tokushima, 1-78-1 Shomachi, Tokushima 770-8505, Japan c Department of Medicinal Chemistry, Kyoto Pharmaceutical University, Yamashina-ku, Kyoto 607-8412, Japan d Lipid Research Group, Gastroenterology, Hepatology and Nutrition Division, The Children’s Hospital of Philadelphia, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, PA 19104-4318, United States a r t i c l e i n f o a b s t r a c t Article history: Apolipoprotein A-I is amenable to a number of specific mutations associated with hereditary systemic amy- Received 6 March 2013 loidoses. Amyloidogenic properties of apoA-I are determined mainly by its N-terminal fragment. In the Received in revised form 8 October 2013 present study Förster resonance energy transfer between tryptophan as a donor and Thioflavin T as an Accepted 25 October 2013 acceptor was employed to obtain struc