Impact of membrane lipid composition on the structure and stability of the transmembrane domain of amyloid precursor protein


Por: Dominguez, Laura, Foster, Leigh, Straub, John E., Thirumalai, D.

Publicada: 6 sep 2016
Categoría: Multidisciplinary

Resumen:
Cleavage of the amyloid precursor protein (APP) by.-secretase is a crucial first step in the evolution of Alzheimer's disease. To discover the cleavage mechanism, it is urgent to predict the structures of APP monomers and dimers in varying membrane environments. We determined the structures of the C99(23-55) monomer and homodimer as a function of membrane lipid composition using a multiscale simulation approach that blends atomistic and coarse-grained models. We demonstrate that the C99(23-55) homodimer structures form a heterogeneous ensemble with multiple conformational states, each stabilized by characteristic interpeptide interactions. The relative probabilities of each conformational state are sensitive to the membrane environment, leading to substantial variation in homodimer peptide structure as a function of membrane lipid composition or the presence of an anionic lipid environment. In contrast, the helicity of the transmembrane domain of monomeric C99(1-55) is relatively insensitive to the membrane lipid composition, in agreement with experimental observations. The dimer structures of human EphA2 receptor depend on the lipid environment, which we show is linked to the location of the structural motifs in the dimer interface, thereby establishing that both sequence and membrane composition modulate the complete energy landscape of membrane-bound proteins. As a by-product of our work, we explain the discrepancy in structures predicted for C99 congener homodimers in membrane and micelle environments. Our study provides insight into the observed dependence of C99 protein cleavage by.-secretase, critical to the formation of amyloid-beta protein, on membrane thickness and lipid composition.

Filiaciones:
Dominguez, Laura:
 Boston Univ, Dept Chem, Boston, MA 02215 USA

 Univ Nacl Autonoma Mexico, Sch Chem, Dept Phys Chem, Mexico City 04510, DF, Mexico

Foster, Leigh:
 Boston Univ, Dept Chem, Boston, MA 02215 USA

Straub, John E.:
 Boston Univ, Dept Chem, Boston, MA 02215 USA

Thirumalai, D.:
 Univ Texas Austin, Dept Chem, Austin, TX 78712 USA
ISSN: 00278424
Editorial
NATL ACAD SCIENCES, 2101 CONSTITUTION AVE NW, WASHINGTON, DC 20418 USA, Estados Unidos America
Tipo de documento: Article
Volumen: 113 Número: 36
Páginas: 5281-5287
WOS Id: 000383094500007
ID de PubMed: 27559086