Biomedical subjects

Andreas Erbe

Publications and source records attributed to Andreas Erbe.

3 recordsLinked to original sources

PubMed2007

Ion distribution around electrostatically stabilized polystyrene latex particles studied by ellipsometric light scattering.

The ion distribution around electrostatically stabilized polystyrene latex spheres for different ionic strengths is investigated by ellipsometric light scattering. This method is sensitive to the refractive index profile around colloidal particles, which is affected by the local salt content. At an average salt concentration of c* = 10(-4) mol L(-1), the ion concentration at the particle interface increases discontinuously, and a layer of high salt content with 20-30 nm thickness is built up. The observation cannot be explained within the framework of the Poisson-Boltzmann equation; it rather resembles a prewetting transition. Interactions that could possibly lead to a stabilization of the observed layer of high salt content are discussed.

Journal Article↗

PubMed2006

Ellipsometric light scattering for the characterization of thin layers on dispersed colloidal particles.

The thin interface layer on colloids in a liquid can be characterized by applying nulling ellipsometry to a scattering experiment. Close to 90 degrees scattering angle the ellipsometric quantities tan(Psi) and Delta of particles smaller than the wavelength behave like at the Brewster angle of reflection ellipsometry. The minimum of tan(Psi) and the slope of Delta depend on thickness and refractive index of the layer, while the location of the minimum is sensitive to the refractive index of the particle. As an example, the swelling of a thermosensitive layer on colloidal particles has been determined from measurements at two wavelengths.

Journal Article↗

PubMed2004

Infrared reflection absorption spectroscopy of amphipathic model peptides at the air/water interface.

The linear sequence KLAL (KLALKLALKALKAALKLA-NH(2)) and its corresponding d,l-isomers k(9)a(10)-KLAL (KLALKLALkaLKAALKLA-NH(2)) and l(11)k(12)-KLAL (KLALKLALKAlkAALKLA-NH(2)) are model compounds for potentially amphipathic alpha-helical peptides which are able to bind to membranes and to increase the membrane permeability in a structure- and target-dependent manner (Dathe and Wieprecht, 1999) We first studied the secondary structure of KLAL and its analogs bound to the air/water using infrared reflection absorption spectroscopy. For the peptide films the shape and position of the amide I and amide II bands indicate that the KLAL adopts at large areas per molecule an alpha-helical secondary structure, whereas at higher surface pressures or smaller areas it converts into a beta-sheet structure. This transition could be observed in the compression isotherm as well as during the adsorption at the air/water interface from the subphase as a function of time. The secondary structures are essentially orientated parallel to the air/water interface. The analogs with d-amino acids in two different positions of the sequence, k(9)a(10)-KLAL and l(11)k(12)-KLAL, form only beta-sheet structures at all surface pressures. The observed results are interpreted using a comparison of hydrophobic moments calculated for alpha-helices and beta-sheets. The differences between the hydrophobic moments calculated using the consensus scale are not large. Using the optimal matching hydrophobicity scale or the whole-residue hydrophobicity scale the beta-sheet even has the larger hydrophobic moment.

Adsorption↗