The rheological properties of beta amyloid Langmuir monolayers:Comparative studies with melittin peptide

CARUSO, B.,; AMBROGGIO E.E.,; WILKE, N.,; FIDELIO G.D.

COLLOIDS AND SURFACES B-BIOINTERFACES

ELSEVIER SCIENCE BV

Lugar: Amsterdam; Año: 2016 vol. 146 p. 180 - 180

0927-7765

!--[if gte mso 9]> 1024x768 We determined the rheological properties of β-amyloid Langmuir films at the air/water interface, a peptide whose interfacial structure is extended β-sheet, and compared them with those of films composed of Melittin (Mel), which adopts an α-helical conformation at neutral pH. To determine the dilatational and shear moduli we evaluated the response of pure peptide monolayers to an oscillatory anisotropic compressive work. Additionally, a micro-rheological characterization was performed by tracking the diffusion of micrometer sized latex beads onto the interface. This technique allowed us the detection of different rheological behaviour between monolayers presenting a low shear response. Monolayers of the β-sheet structure-adopting peptides, such as β-amyloid peptides, exhibited a marked shear (elastic)