@article { ISI:000253014400014,
	title = {Protection of oligo deoxynucleotides against nuclease degradation through association with self-assembling peptides},
	journal = {Biomaterials},
	volume = {29},
	number = {8},
	year = {2008},
	month = {MAR},
	pages = {1099-1108},
	publisher = {ELSEVIER SCI LTD},
	address = {THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLAND},
	abstract = {<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>},
	keywords = {aggregate, centrifugation, Fluorescence resonance energy transfer (FRET), nuclease resistance, oligonucleotide, self-assembling peptide},
	issn = {0142-9612},
	doi = {10.1016/j.biomaterials.2007.10.049},
	author = {Wang, M. and Adikane, H. V. and Duhamel, J. and Chen, P.}
}
@article { ISI:000288576700003,
	title = {Fluorescence resonance energy transfer from tryptophan to folic acid in micellar media and deionised water},
	journal = {Journal of Photochemistry and Photobiology B-Biology},
	volume = {103},
	number = {1},
	year = {2011},
	month = {APR},
	pages = {16-21},
	publisher = {ELSEVIER SCIENCE SA},
	address = {PO BOX 564, 1001 LAUSANNE, SWITZERLAND},
	abstract = {<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>},
	keywords = {Fluorescence quenching, Fluorescence resonance energy transfer (FRET), Folic acid, Foster theory, Stern-Volmer plot, Tryptophan},
	issn = {1011-1344},
	doi = {10.1016/j.jphotobiol.2011.01.006},
	author = {Mote, U. S. and Patil, S. R. and Bhosale, Siddharth H. and Han, Sung-Hwan and Kolekar, G. B.}
}
