02379nas a2200253   4500008004100000022001400041245012000055210006900175260009900244300001400343490000700357520141500364653001401779653001901793653005001812653002401862653002001886653002801906100001301934700002001947700001601967700001301983856012901996       2008                        eng d  a0142-961200aProtection of oligo deoxynucleotides against nuclease degradation through association with self-assembling peptides0 aProtection of oligo deoxynucleotides against nuclease degradatio  aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLANDbELSEVIER SCI LTDcMAR  a1099-11080 v293 a<p>Aggregates of the self-assembling peptide EAK16II or EAK16IV and oligodeoxynucleotides (ODNs) were prepared, and their stability upon diluting the solution was investigated by UV-vis spectroscopy. The aggregates prepared at pH 4 and pH 7 did not dissociate after the solution was diluted 5- and 10-fold. The resistance against Escherichia coli exonuclease I of the ODN located in the EAK-ODN aggregates was studied by fluorescence resonance energy transfer (FRET) after the ODN had aggregated with EAK 16II or EAK 16IV at pH 4 or pH 7. The effect that the peptide sequence, peptide concentration, pH, and centrifugation had on protecting the aggregated ODN against nuclease degradation was investigated. Significant nuclease resistance was obtained after the EAK-ODN aggregates had been prepared at pH 4, with an EAK16IV concentration greater than a threshold value, and ensuring that the solution was not centrifuged immediately after sample preparation. Centrifuging the EAK16IV-ODN solution immediately after sample preparation resulted in the loss of this nuclease protection. However, if the solution of EAK-ODN aggregates was centrifuged 24h after sample preparation, the nuclease protection afforded by the EAK16IV-ODN aggregates to the ODN was maintained even after being subject to a 10-fold dilution and up to 4 rounds of centrifugation over 4 days. (c) 2007 Elsevier Ltd. All rights reserved.</p>10aaggregate10acentrifugation10aFluorescence resonance energy transfer (FRET)10anuclease resistance10aoligonucleotide10aself-assembling peptide1 aWang, M.1 aAdikane, H., V.1 aDuhamel, J.1 aChen, P.  uhttps://library.ncl.res.in/content/protection-oligo-deoxynucleotides-against-nuclease-degradation-through-association-self-001853nas a2200265   4500008004100000022001400041245011100055210006900166260006900235300001000304490000800314520088600322653002701208653005001235653001501285653001801300653002201318653001501340100001701355700001801372700002701390700001901417700002001436856013101456       2011                        eng d  a1011-134400aFluorescence resonance energy transfer from tryptophan to folic acid in micellar media and deionised water0 aFluorescence resonance energy transfer from tryptophan to folic   aPO BOX 564, 1001 LAUSANNE, SWITZERLANDbELSEVIER SCIENCE SAcAPR  a16-210 v1033 a<p>The fluorescence resonance energy transfer (FRET) from tryptophan (Trp) to folic acid (FA) in aqueous sodiumdodecyl sulphate, cetyltrimethyl ammonium bromide, and Brij-35 as well as deionised water was investigated using steady state and time resolved fluorescence techniques. The data obtained from steady state fluorescence spectral studies and time resolved measurement indicated that the FRET from Trp to FA occurred most effectively in aqueous sodium dodecyl sulphate micellar solutions. The distance between Trp and FA were evaluated. Binding constant, number of binding sites and thermodynamic parameters were determined for Trp-FA interactions in deionised water. The values of the thermodynamic parameters suggest that the hydrophobic forces and hydrogen bonding are the key interacting forces between Trp-FA interaction. (C) 2011 Elsevier B.V. All rights reserved.</p>10aFluorescence quenching10aFluorescence resonance energy transfer (FRET)10aFolic acid10aFoster theory10aStern-Volmer plot10aTryptophan1 aMote, U., S.1 aPatil, S., R.1 aBhosale, Siddharth, H.1 aHan, Sung-Hwan1 aKolekar, G., B.  uhttps://library.ncl.res.in/content/fluorescence-resonance-energy-transfer-tryptophan-folic-acid-micellar-media-and-deionised-0