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Structural characterization of the model amphipathic peptide Ac-LKKLLKLLKKLLKL-N[H.sub.2] in aqueous solution and with 2,2,2-trifluoroethanol and 1,1,1,3,3,3-hexafluoroisopropanol

Authors :
Buchko, Garry W.
Jain, Avijita
Reback, Matthew L.
Shaw, Wendy J.
Source :
Canadian Journal of Chemistry. June 1, 2013, Vol. 91 Issue 6, p406, 8 p.
Publication Year :
2013

Abstract

Short-chain amphipathic peptides are promising components in the new generation of engineered biomaterials. The model 14-residue leucine-lysine peptide Ac-LKKLLKLLKKLLKL-N[H.sub.2] (LKα) is one such amphipathic peptide. In dilute aqueous solution ( Key words: biomaterials, amphipathic peptide, NMR spectroscopy, circular dichroism spectroscopy, fluorinated alcohols. Resume : Les peptides amphipathiques a chame courte sont des composes tres prometteurs qui font partie de la nouvelle generation de produits issus du genie des biomateriaux. Le peptide modele contenant 14 residus leucine et lysine AcLKKLLKLLKKLLKL-N[H.sub.2] (LKα) est l'un d'entre eux. On a suggere anterieurement, en s'appuyant sur des donnees de spectroscopie DC, qu'en solution aqueuse diluee ( Mots-cles: biomateriaux, peptide amphipathique, spectroscopie RMN, spectroscopie de dichroisme circulaire, alcools fluores.<br />Introduction Peptides play a wide variety of biochemical roles in multicellular organisms, ranging from weapons for antimicrobial destruction (1) to messengers for intercellular communication. (2) Their biological importance is highlighted [...]

Details

Language :
English
ISSN :
00084042
Volume :
91
Issue :
6
Database :
Gale General OneFile
Journal :
Canadian Journal of Chemistry
Publication Type :
Academic Journal
Accession number :
edsgcl.336177229
Full Text :
https://doi.org/10.1139/cjc-2012-0429