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PL
Celem niniejszej pracy była próba określenia wpływu wybranych czynników/parametrów na wynik maksymalnego przepływu nosowego wdechowego (PNIF, ang. peak nasal inspiratory flow) w badanej populacji polskiej projektu Epidemiologia Chorób Alergicznych w Polsce (ECAP). Materiał/metody: Badaną populację stanowiła grupa dzieci w wieku 6–7 lat (n=1123), młodzieży w wieku 13–14 lat (n=1136) oraz dorosłych (n=1876) zamieszkałych w siedmiu dużych polskich miastach. W badaniu posłużono się pomiarem maksymalnego przepływu nosowego wdechowego (PNIF). Do oceny wpływu wybranych czynników na wartości PNIF wykorzystano przetłumaczone i walidowane kwestionariusze opracowane na potrzeby światowych badań ECRHS II (European Community Respiratory Health Survey II) i ISAAC (International Study of Asthma and Allergies in Childhood). Wyniki: Określone warunki wewnątrz gospodarstwa domowego, m.in. ogrzewanie węglem, drewnem lub piecem gazowym, istotnie zwiększają przekrwienie błony śluzowej nosa. W grupie biernych palaczy PNIF był niższy niż w grupie czynnych palaczy. Wskaźnik PNIF malał wraz ze wzrostem liczby domowników palących papierosy. Wnioski: Wybrane czynniki środowiska
EN
The aim of this study was to investigate the effect of selected factors/parameters on peak nasal inspiratory flow (PNIF) in the Polish population as part of the Epidemiology of Allergic Diseases in Poland study. Material/methods: The popu¬lation of this study comprised of a group of children aged 6–7 years (n=1123), adolescents aged 13–14 years (n=1136), and adults (n=1876) – all residents of seven large Polish cities. Method – measurement of PNIF. The effect of selected param¬eters on PNIF was measured with translated and validated questionnaires developed for international studies ECRHS II (European Community Respiratory Health Survey II) and ISAAC (International Study of Asthma and Allergies in Child¬hood). Results: Indoor environmental factors including heating with coal, wood or gas significantly increase nasal con¬gestion. In the group of passive smokers, PNIF was lower than in the group of active smokers. PNIF rate decreased with the number of smokers per household. Conclusions: Peak nasal inspiratory flow values were significantly affected by such parameters as selected household environmental factors.
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Supramolecularity creates nonstandard protein ligands

86%
EN
Congo red and a group of structurally related dyes long used to stain amyloid proteins are known to associate in water solutions. The self-association of some dyes belonging to this group appears particularly strong. In water solutions their molecules are arranged in ribbon-like micellar forms with liquid crystalline properties. These compounds have recently been found to form complexeswith some native proteins in a non-standard way. Gaps formed by the local distribution of β-sheets in proteins probably represent the receptor sites for these dye ligands. They may result from higher structural instability in unfolding conditions, but also may appear as long range cooperative fluctuations generated by ligand binding. Immunoglobulins G were chosen as model binding proteins to check the mechanism of binding of these dyes. The sites of structural changes generated by antigen binding in antibodies, believed to act as a signal propagated to distant parts of the molecule, were assumed to be suitable sites for the complexation of liquid-crystalline dyes. This assumption was confirmed by proving that antibodies engaged in immune complexation really do bind these dyes; as expected, this binding affects their function by significantly enhancing antigen binding and simultaneously inhibiting C1q attachment. Binding of these supramolecular dyes by some other native proteins including serpins and their natural complexes was also shown. The strict dependence of the ligation properties on strong self-assembling and the particular arrangement of dye molecules indicate that supramolecularity is the feature that creates non-standard protein ligands, with potential uses in medicine and experimental science.
EN
Congo red (CR) is a known selective amyloid ligand. The focus of our work is identification (by EM imaging) of dye binding sites and their distribution in amyloids and amyloid-like aggregates formed in vitro. In order to produce the required contrast, CR has been indirectly combined with metal via including Titan yellow (TY) by intercalation which exhibits a relatively strong affinity for silver ions. The resulting combined ligand retains its ability to bind to proteins (which it owes to CR) and can easily be detected in EM studies thanks to TY. We have found, however, that in protein aggregates where unfolding is stabilized by aggregation and therefore is irreversible, TY alone may serve as both, the ligand and the metal carrier. The formation of ordered structures in amyloids was studied using IgG light chains with amyloidogenic properties, converted into amyloids by shaking. The resulting EM images were subjected to interpretation on the basis of the authors' earlier research on the CR/light chain complexation process. Our results indicate that dimeric light chains, which are the subject of our study, produce amyloids or amyloid-like complexes with chain-like properties and strong helicalization tendencies. Cursory analysis suggests that the edge polypeptide loops belonging to unstable light chains form intermolecular bridges which promote creation of loose gel deposits, or are otherwise engaged in the swapping processes leading to higher structural ordering.
EN
The self-assembling tendency and protein complexation capability of dyes related to Congo red and also some dyes of different structure were compared to explain the mechanism of Congo red binding and the reason for its specific affinity for β-structure. Complexation with proteins was measured directly and expressed as the number of dye molecules bound to heat-aggregated IgG and to two light chains with different structural stability. Binding of dyes to rabbit antibodies was measured indirectly as the enhancement effect of the dye on immune complex formation. Self-assembling was tested using dynamic light scattering to measure the size of the supramolecular assemblies. In general the results show that the supramolecular form of a dye is the main factor determining its complexation capability. Dyes that in their compact supramolecular organization are ribbon-shaped may adhere to polypeptides of β-conformation due to the architectural compatibility in this unique structural form. The optimal fit in complexation seems to depend on two contradictory factors involving, on the one hand, the compactness of the non-covalently stabilized supramolecular ligand, and the dynamic character producing its plasticity on the other. As a result, the highest protein binding capability is shown by dyes with a moderate self-assembling tendency, while those arranging into either very rigid or very unstable supramolecular entities are less able to bind.
EN
This study describes a technique which makes it possible to introduce the amyloid-like order to protein aggregates by using the scaffolding framework built from supramolecular, fibrillar Congo red structures arranged in an electric field. The electric field was used not only to obtain a uniform orientation of the charged dye fibrils, but also to make the fibrils long, compact and rigid due to the delocalization of pi electrons, which favors ring stacking and, as a consequence, results in an increased tendency to self-assemble. The protein molecules (immunoglobulin L chain lambda, ferritin) attached to this easily adsorbing dye framework assume its ordered structure. The complex precipitating as plate-like fragments shows birefringence in polarized light. The parallel organization of fibrils can be observed with an electron microscope. The dye framework may be removed via reduction with sodium dithionite, leaving the aggregated protein molecules in the ordered state, as confirmed by X-ray diffraction studies. [...]
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