Step-scan Michelson Fourier-transform spectrometer for optical emission spectroscopy in UV-VIS spectral range.

We present the design, construction, and first spectra of a step-scan Michelson Fourier-transform spectrometer for optical emission spectroscopy in the UV-VIS spectral range. The mirror motion mechanism is based on a long-travel piezo-based linear translation stage with built-in position feedback. The step-scan arrangement allows for signal integration, making the instrument suitable for measurements of less intensive radiation sources and for the photon-counting technique.

5'-Nucleotidase from Vipera lebetina venom.

5'-Nucleotidase (5'-NT) is widely represented in animal tissues (CD73) as well as in almost all snake venoms. In the present study, a 5'-NT isoform has been isolated from Vipera lebetina venom. The homodimeric isoform consists of monomers with molecular masses of 60 kDa.

Phosphodiesterase from Vipera lebetina venom - structure and characterization.

Nucleases and phosphatases are ubiquitous but mostly marginal components of snake venoms. These proteins have been studied quite extensively but up to now no data regarding their amino acid sequences confirmed at protein level have been published. The present study deals with purification, characterization, and structural properties of a phosphodiesterase from Vipera lebetina venom (VLPDE).

The natural product betulinic acid rapidly promotes amyloid-β fibril formation at the expense of soluble oligomers.

The biochemical hallmarks of Alzheimer’s disease (AD) are the aggregates of amyloid-β (Aβ) peptide that deposit in brains of AD patients as senile plaques. The monomeric Aβ undergoes aggregation in a nucleation-dependent manner to form insoluble fibrils. Emerging evidence suggests that the low-molecular-weight aggregates called “soluble oligomers” are the primary neurotoxic agents as opposed to the fibrils.

Interactions of PLA2-s from Vipera lebetina, Vipera berus berus and Naja naja oxiana venom with platelets, bacterial and cancer cells.

Secretory phospholipasesA(2) (sPLA(2)s) form a large family of structurally related enzymes widespread in nature. Herein, we studied the inhibitory effects of sPLA(2)s from Vipera lebetina (VLPLA(2)), Vipera berus berus (VBBPLA(2)), and Naja naja oxiana (NNOPLA(2)) venoms on (i) human platelets, (ii) four different bacterial strains (gram-negative Escherichia coli and Vibrio fischeri; gram-positive Staphylococcus aureus and Bacillus subtilis) and (iii) five types of cancer cells (PC-3, LNCaP, MCF-7, K-562 and B16-F10) in vitro. sPLA(2)s inhibited collagen-induced platelet aggregation: VBBPLA(2) IC(50) = 0.