Gangliosides binding peptide

Yahi N, Fantini J. Deciphering the glycolipid code of Alzheimer s and Parkinson s amyloid proteins allowed the creation of a universal ganglioside-binding Peptide. PloS One. 2014 9(8) el04751. 

Matsubara T, Ishikawa D, Taki T, Okahata X Sato T. Selection of ganglioside GMl-binding peptides by using a phage Hbrary. FEBS Lett. 1999 456(2) 253-256. 

The nonpolar ceramide chains of the ganglioside are buried in the membrane bilayer. The initial tight binding (fQ 2 x 107 M-1) of the toxin is followed by a poorly understood process in which the A subunit enters the cell. The peptide chain of this subunit is... 

Cholera toxin interrupts the GTPase-switching cycle of the G, of intestinal epithelial cells, thereby causing the massive water loss from the body that is characteristic of cholera victims. It is composed of an A-subunit, consisting of an Aj-peptide (23 kDa) linked to an A2-peptide by an -S- bridge, and five B-subunits. The latter bind specifically to the Gmi ganglioside located on the luminal surface of the plas-... 

Fantini J, Yahi N, Garmy N. Cholesterol accelerates the binding of Alzheimer s beta-amyloid peptide to ganglioside GMl through a universal hydrogen-bond-dependent sterol tuning of glycoUpid conformation. Front Physiol. 2013 4 120. 

FIGURE 8.5 Structuration of an IDP upon binding to membrane lipids. When an IDP comes close to a membrane, specific interactions with selected lipids (such as gangliosides in lipid rafts) will favor the efficient adhesion of the protein to this membrane. Moreover, the repetitive head groups of raft lipids wiU induce a-helical folding of the protein through a typical chaperone-facilitated reaction. The reduction of dimensionality from 3D (extracellular milieu) to 2D (hpid raft surface) also favors the concentration of the protein on the membrane surface. The Parkinson s and Alzheimer s disease-associated proteins a-synuclein and p-amyloid peptides (Ap) are typical examples of such IDPs that acquire a helical structure when bound to hpid rafts of neural cells. 

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