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The scaling exponents alpha, beta, and 1/z in thin films of the organic molecule diindenoperylene deposited on SiO2 under UHV conditions are determined. Atomic-force microscopy, x-ray reflectivity, and diffuse x-ray scattering were employed. The surface width displays power law scaling over more than 2 orders of magnitude in film thickness. We obtained alpha = 0.684+/-0.06, beta = 0.748+/-0.05, and 1/zeta = 0.92+/-0.20. The derived exponents point to an unusually rapid growth of vertical roughness and lateral correlations. We suggest that they could be related to lateral inhomogeneities arising from the formation of grain boundaries between tilt domains in the early stages of growth.

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The islet amyloid polypeptide (IAPP) or amylin is a pancreatic hormone and crucially involved in the pathogenesis of type-II diabetes mellitus (T2DM). Aggregation and amyloid formation of IAPP is considered as the primary culprit for pancreatic beta-cell loss in T2DM patients. In this study, first X-ray reflectivity (XRR) measurements on IAPP at lipid interfaces have been carried out, providing a molecular level characterization of the first steps of the lipid-induced fibrillation process of IAPP, which is initiated by lipid-induced nucleation, oligomerization, followed by detachment of larger IAPP aggregate structures from the lipid membrane, and terminated by the formation of mature fibrils in the bulk solution. The adsorption process of IAPP at lipid interfaces in the absence and presence of negatively charged lipid has also been studied by complementary ATR-FTIR spectroscopic measurements. The morphological properties were followed by atomic force microscopy (AFM). Moreover, we show that the polyphenolic red wine compound resveratrol is able to inhibit IAPP aggregation also in the presence of aggregation-fostering negatively charged lipid interfaces, revealing its potential as a drug candidate for T2DM.