ACS Omega

Structural characterization of the amyloid precursor protein transmembrane domain and its gamma-cleavage site

Anna Itkin,  Evgeniy S. Salnikov, Christopher Aisenbrey, Jesus Raya, Elise Glattard, Vincent Raussens, Jean-Marie Ruysschaert, Burkhard Bechinger

ACS Omega, 2017, 2 (10), pp 6525–6534 (team Membrane biophysics and NMR):

 

Alzheimer’s disease is the most common form of dementia that affects about 50 million of sufferers worldwide. A major role for the initiation and progression of Alzheimer’s disease has been associated with the amyloid β-peptide (Aβ), which is a protease cleavage product of the amyloid precursor protein. The amyloid precursor protein is an integral membrane protein with a single transmembrane domain. In the context of a European research and training network the NMR team of the UMR7177 and their collaborators from the Free University of Brussels investigated the structural integrity of the transmembrane domain within lipid bilayers, and determined the tilt angle distribution and dynamics of various subdomains using oriented solid-state NMR and ATR-FTIR spectroscopies. Importantly, pronounced conformational and topological heterogeneity were observed for the g- and, to a lesser extent, the z-cleavage site, with pronounced implications for the production of Aβ and related peptides.

Contact chercheur:

Burkhard Bechinger, Institut de Chimie de Strasbourg

Courriel: bechinge@unistra.fr