6 research outputs found
Засоби масової комунікації в культурі суспільства постмодерну
Проаналізовано місце, роль та вплив засобів масової комунікації на суспільство й індивіда в умовах інформаційного суспільства.Проанализировано место, роль и влияние средств массовой коммуникации на общество и индивида в условиях информационного общества.A place, role and influencing of facilities of mass communication, is analized on society and individual in the conditions of informative societ
Activation of phospholipase A2 by Hsp70 in vitro
Corrigendum to “Activation of phospholipase A2 by Hsp70 in vitro” Biochimica et Biophysica Acta (BBA) – Biomembranes Vol. 1838, Issue 7, July 2014, Pages 1921 10.1016/j.bbamem.2014.03.020Peer reviewe
Binding of amphipathic α-helical antimicrobial peptides to lipid membranes: Lessons from temporins B and L
AbstractTemporins constitute a family of amphipathic α-helical antimicrobial peptides (AMP) and contain some of the shortest cytotoxic peptides, comprised of only 10–14 residues. General characteristics of temporins parallel those of other AMP, both in terms of structural features and biophysical properties relating to their interactions with membrane lipids, with selective lipid-binding properties believed to underlie the discrimination between target vs host cells. Lipid-binding properties also contribute to the cytotoxicity AMP, causing permeabilization of their target cell membranes. The latter functional property of AMP involves highly interdependent acidic phospholipid-induced conformational changes, aggregation, and formation of toxic oligomers in the membrane. These oligomers are subsequently converted to amyloid-type fibers, as demonstrated for e.g. temporins B and L in our laboratory, and more recently for dermaseptins by Auvynet et al. Amyloid state represents the generic minimum in the folding/aggregation free energy landscape, and for AMP its formation most likely serves to detoxify the peptides, in keeping with the current consensus on mature amyloid being inert and non-toxic. The above scenario is supported by sequence analyses of temporins as well as other amphipathic α-helical AMP belonging to diverse families. Accordingly, sequence comparison identifies ‘conformational switches’, domains with equal probabilities for adopting random coil, α-helical and β-sheet structures. These regions were further predicted also to aggregate and assemble into amyloid β-sheets. Taken together, the lipid-binding properties and structural characterization lend support to the notion that the mechanism of membrane permeabilization by temporins B and L and perhaps of most AMP could be very similar, if not identical, to that of the paradigm amyloid forming cytotoxic peptides, responsible for degenerative cell loss in e.g. prion, Alzheimer's and Parkinson's disease, and type 2 diabetes