SignificanceToday, more than 40 million people worldwide are affected by neurodegenerative disorders. These diseases are associated at the molecular level with the aggregation of specific proteins into insoluble fibrils, termed amyloids. Increasing evidence suggests that the intermediate aggregates, rather than the final fibrillar products, are implicated in toxicity in vivo. However, the investigation of the conversion of proteins into amyloids represents a formidable experimental challenge because of their nanoscale and heterogeneous nature. Here, we report the identification of a mechanism of early assembly of monomeric proteins into elongated intermediates during amyloid formation. The biophysical characterization of novel intermediate molecular species is fundamental to unravel their mechanism of formation and gain insights into their potential toxicity and role in pathology.

Currently, sensors invade into our everyday life to bring higher life standards, excellent medical diagnostic and efficient security. Plasmonic biosensors demonstrate an outstanding performance ranking themselves among best candidates for different applications. However, their sensitivity is still limited that prevents further expansion. Here we present a novel concept of magnetoplasmonic sensor with ultranarrow resonances and high sensitivity. Our approach is based on the combination of a specially designed one-dimensional photonic crystal and a ferromagnetic layer to realize ultralong-range propagating magnetoplasmons and to detect alteration of the environment refractive index via observation of the modifications in the Transversal Magnetooptical Kerr Effect spectrum. The fabrication of such a structure is relatively easy in comparison with e.g. nanopatterned samples. The fabricated heterostructure shows extremely sharp (angular width of 0.06°) surface plasmon resonance and even sharper magnetoplasmonic resonance (angular width is 0.02°). It corresponds to the propagation length as large as 106 μm which is record for magnetoplasmons and promising for magneto-optical interferometry and plasmonic circuitry as well as magnetic field sensing. The magnitude of the Kerr effect of 11% is achieved which allows for detection limit of 1∙10−6. The prospects of further increase of the sensitivity of this approach are discussed.

Atomic force microscopy was used to image singlestranded DNA (ssDNA) adsorbed on mica modified by Mg 2+ , by 3-aminopropyltriethoxysilane or on modified highly oriented pyrolytic graphite (HOPG). ssDNA molecules on mica have compact structures with lumps, loops and super twisting, while on modified HOPG graphite ssDNA molecules adopt a conformation without secondary structures. We have shown that the immobilization of ssDNA under standard conditions on modified HOPG eliminates intramolecular base-pairing, thus this method could be important for studying certain processes involving ssDNA in more details.

A label-free biosensor device based on registration of photonic crystal surface waves is described. Angular interrogation of the optical surface wave resonance is used to detect changes in the thickness of an adsorbed layer, while an additional simultaneous detection of the critical angle of total internal reflection provides independent data of the liquid refractive index. The abilities of the device are demonstrated by measuring of biotin molecule binding to a streptavidin monolayer, and by measuring association and dissociation kinetics of immunoglobulin G proteins. Additionally, deposition of PSS/PAH polyelectrolytes is recorded in situ resulting calculation of PSS and PAH monolayer thicknesses separately.

A new method of direct and continuous measurement of the spring constant of single molecule or molecular complex is elaborated. To that end the standard force spectroscopy technique with functionalized tips and samples is combined with a small dithering of the tip. The change of the dithering amplitude as a function of the pulling force is measured to extract the spring constant of the complex. The potentialities of this method are illustrated for the experiments with single bovine serum albumin-its polyclonal antibody (Ab-BSA) and fibrinogen-fibrinogen complexes.