Study of carotenoids in cyanobacteria by Raman spectroscopy.

Cyanobacteria have established dominant aquatic populations around the world, generally in aggressive environments and under severe stress conditions, e.g., intense solar radiation. Several marine strains make use of compounds such as the polyenic molecules for their damage protection justifying the range of colours observed for these species. The peridinin/chlorophyll-a/protein complex is an excellent example of essential structures used for self-prevention; their systems allow to them surviving under aggressive environments. In our simulations, few protective dyes are required to the initial specimen defense; this is an important data concern the synthetic priority in order to supply adequate damage protection. Raman measurements obtained with 1064 and 514.5 nm excitations for Cylindrospermopsis raciborskii and Microcystis aeruginosa strains shows bands assignable to the carotenoid peridinin. It was characterized by bands at 1940, 1650, 1515, 1449, 1185, 1155 and 1000 cm(-1) assigned to ν(C=C=C) (allenic vibration), ν(C=C/CO), ν(C=C), δ(C-H, C-18/19), δ(C-H), ν(C-C), and ρ(C-CH3), respectively. Recognition by Raman spectroscopy proved to be an important tool for preliminaries detections and characterization of polyene molecules in several algae, besides initiate an interesting discussion about their synthetic priority.

Biophysical and morphological studies on the dual interaction of non-octarepeat prion protein peptides with copper and nucleic acids.

Conversion of prion protein (PrP) to an altered conformer, the scrapie PrP (PrP(Sc)), is a critical step in the development of transmissible spongiform encephalopathies. Both Cu(II) and nucleic acid molecules have been implicated in this conversion. Full-length PrP can bind up to six copper ions; four Cu(II) binding sites are located in the octarepeat domain (residues 60-91), and His-96 and His-111 coordinate two additional copper ions. Experimental evidence shows that PrP binds different molecules, resulting in diverse cellular signaling events. However, there is little information about the interaction of macromolecular ligands with Cu(II)-bound PrP. Both RNA and DNA sequences can bind PrP, and this interaction results in reciprocal conformational changes. Here, we investigated the interaction of Cu(II) and nucleic acids with amyloidogenic non-octarepeat PrP peptide models (comprising human PrP residues 106-126 and hamster PrP residues 109-149) that retain His-111 as the copper-anchoring residue. The effect of Cu(II) and DNA or RNA sequences in the aggregation, conformation, and toxicity of PrP domains was investigated at low and neutral pH. Circular dichroism and EPR spectroscopy data indicate that interaction of the PrP peptides with Cu(II) and DNA occurs at pH 7. This dual interaction induces conformational changes in the peptides, modulating their aggregation, and affecting the morphology of the aggregated species, resulting in different cytotoxic effects. These results provide new insights into the role of Cu(II) and nucleic acid sequences in the structural conversion and aggregation of PrP, which are both critical events related to prion pathogenesis.