The results obtained during the study of mutations on the gene coding for the human prion protein showed that the only major consequence of mutations is the perturbation of the protein surface electrostatic potential which subsequently is responsible for the convergence of PrPc to PrPsc. Streptomycin interacting with the prion protein induce electric charge changes on the prion protein surface leading to loss of infectivity as well the formation of small aggregates.

Neurodegenerative disorders of the central nervous system are slowly developing, insidious conditions that contribute first to neuronal cell degeneration and later cell death. During the development of the spongiform encephalopathies in human and animals the surface cellular glycoprotein (PrPc) undergoes a misfolding conformation, become resistant to proteinase K and in detergents it accumulates as insoluble β-sheet containing aggregates [2,3].

Copyright: © 2016 Moussa A. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Most of the publication studying the effect of cations on the cellular prion protein (PrPc) used either a recombinant PrPc, extracted PrPc from animal organs or in Neuronal cells cultures. Heir is investigated the effect of ions on the pathogenic prion protein proteinase K treated (PrPres) using electrophoresis and western blot.

sc ) via hydrogen bond transfer between each of the guanidine groups and amino acids on one or several peptides and so increases the apparent molecular weight of the protein. With increased quantities and incubation with the PrP sc for one hour at 37°C; these molecules form multimolecular protein aggregates and allowed its recovery via a low centrifugation step. Also other consequences of these interactions are either a drop or even a complete reduction of the prion PrP sc infectivity. These molecules though their interaction with microbes provoked an anti-bacterial activity. The guanidine-containing compounds constitute a very important class of therapeutic agents suitable for the treatment of a wide spectrum of diseases as well as disinfecting agents. Several molecules possesses two guanidine groups as streptomycin, dihydrostreptomycin, triethylenetetramine, bis-3-aminoproylamine, guanidine hydrochloride, and spermine tetra-hydrochloride. The presence of these 2 functional guanidine groups within a non-polymeric hydrophilic molecular system was suspected to be the chemical structure of streptomycin implicated in the interaction with proteins [1]. This interaction takes place through hydrogen bond transfer among the 2 guanidine groups on streptomycin and the amino-acids of one or several prion peptides. The addition of low concentration of streptomycin to a constant amount of non-soluble fraction of the infectious prion protein (PrP sc ) followed by electrophoresis on polyacrylamide gel and immuno detection revealed an increase in the apparent molecular mass of each of the three bands and this increase of the protein molecular mass was proportional to the added streptomycin quantity. When higher streptomycin concentration were added and incubated with PrP sc for one hour at 37°C aggregation and flocculation of the prion protein occurred due to cross-linking by such a proportionally small streptomycin molecule and the PrP sc

Copyright: © 2014 Moussa A . This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. This branch of science is concerned with the study of structures, chemical composition, properties and chemical reactivity of organic compounds and materials. Organic compounds and organic chemicals in biology form the bases of life on our planet and are mainly hydrocarbons but can contain also other elements as oxygen, nitrogen, sulfur, phosphorus, organometallic compounds as sodium, potassium... etc., alkaline earth metals as magnesium, transition metals as Zinc, Copper, Cobalt...etc. or other metals as aluminum.The vital force theory developed before the 19th century differentiated organic compounds obtained from living organisms from the inorganic compounds. Since organic compounds existed often as mixtures, then varieties of techniques were developed for separation, characterization and purity assessment through the following: distillation, crystallization, solvent extraction, mass spectrometry-NMR, centrifugation, electrophoresis and chromatography i.e. HPLC and gas chromatography.

The hydrogen bond transfer between the two guanidine groups present on streptomycin and the different amino acids on the PrPsc peptides provoked changes of the surface electric charges and even probably affected the stability and induced a drop in the PrPsc infectivity. These can explain the reduction to even absence of accumulated prion infectivity marker PrPsc observed at 45 days post intraperitonial inoculation of a mixture of streptomycin and infected mouse brain homogenate of the scrapie strain C506M3 compared to controls.

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To investigate the amplifying potentialities of streptomycin sulfate in the immunohistochemical (IHC) detection of the abnormal prion protein (PrPsc), we used a sequential brain sampling from C506M3 scrapie strain inoculated C57Bl/6 mice. The weekly removed brains, from 7 to 63 days post intra-cranial inoculation were analysed using PrPsc IHC. The introduction of streptomycin sulfate, a technique developed for accurate cellular and regional mapping of PrPsc deposition in several animal TSEs, revealed a substantial amplifying effect and a clear specific PrPsc detection as early as 28 days post inoculation. The location of the first detected PrPsc deposits suggests a possible involvement of the cerebrospinal fluid in the early dissemination of the infectious agent. The meaning of these newly accessible PrPsc deposits is discussed in relation to a possible nascent form of PrPsc molecules detected in situ for the first time. Altogether, these findings argue that this method can be highly useful to study the early stages after infection with prion agents.

The use of streptomycin in the PrP(sc) detection procedures represents a new and attractive way to detect more PrP(sc), the best marker for the transmissible spongiform encephalopathies (TSEs). Actually, the streptomycin PrP(sc) aggregating property reported recently was established as beneficial in PrP(sc) detection using immunohistochemistry in diagnostic as well as in experimental conditions. The present study reports in details how to use advantageously this original streptomycin property in PrP(res) biochemical extraction and detection. Using TSE diagnostic brain material, specificity and increased sensitivity using streptomycin-treated samples were substantiated. Then an early sequential brain and spleen sampling (from 7 to 49 days post-inoculation) from C57Bl/6 mice inoculated intra-cerebrally or intra-peritoneally with C506M3 scrapie strain was analysed using streptomycin versus ultracentrifugation PrP(res) extraction. Whatever the inoculation route, streptomycin allowed earlier PrP(res) detection in spleen (7 d.p.i.), then in brain suggesting a stronger affinity of the infectious agent for the lymphoid compartment.

The use of calix[n]arene derivatives for the sensing of proteins is described. Initially the properties of the calix[n]arenes are described. in order to better understand how the calix[n]arenes may be used for protein sensors, a detailed survey of the interactions between the molecules and amino acids and peptide is presented. The known complexes between proteins and various calix[n]arene derivatives is described and the biological activity of the molecules summarised. The use of calix[n]arenes as protein sensors observed by Schrader using amphiphilic calix[n]arenes shows that these molecules may allow nanomolar sensing. The major section of the work deals with the development of a para-sulfonato-calix[n]arene-based system for the prion protein responsible for bovine spongiform encephalitis and variant-Creutzfeldt-Jacobs disease(v-CJD) in humans. initially, the development of the test was based on a Western Blot detection, however, the need for large scale testing after the discovery that blood transfusion may lead to infection with v-CJD led to the transfer of the technology to an ELISA-based test.

The supramolecular interaction between the pathogenic form of the prion protein and derivatives of the para-sulfonato-calix[n] arenes has been demonstrated and two putative binding sites determined; this interaction leads to an amplification of the Western Blot immunological detection of the prion protein by the SAF84 antibody.