Surface chemistry of Alzheimer's disease: A Langmuir monolayer approach

Molecular Basis for the Glycosphingolipid-Binding Specificity of α-Synuclein: Key Role of Tyrosine 39 in Membrane Insertion

“…Overall, these data indicated that the N-terminal parts of α-synuclein and Aβ share a common motif with high structural homology and significant sequence similarity. Since both the 34-45 fragment of α-synuclein [13][14][15][16][17][18][19][20][21][22][23][24][25][26][27][28][29][30][31], the human cellular prion protein PrP (192-209), a 14-mer GM1-binding peptide selected from a phage display library, and Aβ (fragment [3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20][21]. Identical amino acids are indicated in yellow ( ⁎ ) and amino acids of the same class (conserved substitutions such as basic for basic or aromatic for aromatic) in blue (:).…”

“…The insertion of α-synuclein into each GSL monolayer was quantified by measuring in real time the changes of the surface pressure of the monolayer. 24,30 In the first series of experiments, each GSL monolayer was formed at a mean initial surface pressure of 15 mN m − 1 . The changes in surface pressure (Δπ) were then continuously recorded after the injection of α-synuclein into the subphase (Fig.…”

Comparison between the behavior of different hydrophobic peptides allowing membrane anchoring of proteins

“…Phospholipid monolayers are very useful model membranes to study lipid-protein or lipidpeptide interactions (for a review, see [114][115][116][117][118][119][120][121][122][123][124][125]). Indeed, it allows to control several physical parameters such as the density of lipids and the surface pressure, the subphase content, the lipid composition, etc.…”

“…One can wonder whether the same results can be obtained with these two approaches and which one is most appropriate. There is approximately twice as many papers reporting measurements where peptides are injected into the subphase [105,125,176,192, as compared to papers reporting data after spreading lipid-peptide mixtures at the air-water interface [176-178, 180-185, 190, 191, 193, 194, 218, 220, 229, 289, 295-326]. It is most relevant to find out whether the same peptide structure is obtained when using these two approaches.…”

Self-assembly of short amyloidogenic peptides at the air–water interface

“…Several amyloid-forming peptides and proteins are surface-active [24][25][26][27][28][29]. Interaction of amyloid-forming proteins and peptides with membranes [30][31][32][33][34][35][36] and lipid monolayers [37][38][39] has been investigated.…”