Systems suitable for the effective preparation of complexes with siRNA (small interfering RNA) are at the center of interest in the area of research work on the delivery of the RNA-based drugs (RNA-therapeutics). This article presents results of a study on the structural effects associated with siRNA complexation by a surfactant comprising a lactose group (N-(3-propanesulfone)-N-dodecyl-amino-beta-D-lactose hydrochloride, LA12). The double stranded siRNA oligomer (21 base pairs) used in this study is responsible for silencing a gene that can be important in the therapy of myotonic dystrophy type 1. The obtained siRNA/LA12 lipoplexes were studied using the methods of small angle scattering of synchrotron radiation, circular dichroism spectroscopy, Fourier transform infrared spectroscopy, and electrophoretic mobility tests. Lipoplexes form in solution stable lamellar or cubic phases. The surfactant selected for the study shows much lower cytotoxicity and good complexation abilities of siRNA than dicationic or polycationic surfactants.
In this work we studied the effects produced by green and red light on two proteins: b L-crystallin and ovalbumin. We evaluated these changes by the calorimetric response, particle size distribution, secondary structure, and fluorescence emission. The main result is the aggregation on b L-crystallin and the increase in cohesion in both proteins. Our work may advance our understanding about structural and aggregation processes in proteins subjected to visible radiation and the possible relation to cataract formation. Our findings show that components of lower energy than blue light may be also of some concern.
topoisomerase I assays and mung bean nuclease assays. The topoisomerase I assays suggest that NQO unwinds the DNA upon binding. NQO/DNA bp ratios from 0.07 to 0.3 produced enhancement in mung bean nuclease activity. NQO/DNA bp ratios from 0.7 to 3 produced inhibited cleavage. This change in effect with concentration may indicate cooperativity in NQO binding. These assays provide further indication that NQO distorts the structure of DNA -which could lead to the changes in restriction enzyme activity. The results presented provide further insight into the modes of carcinogen attack on DNA.
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