June 3, 2013
Journal Article

Structural characterization of the model amphipathic peptide Ac-LKKLLKLLKKLLKL-NH2 in aqueous solution and with 2,2,2-trifluoroethanol and 1,1,1,3,3,3-hexafluoroisopropanol

Abstract

Short-chain amphiphilic peptides are promising components in the new generation of engineered biomaterials with many potential applications. The 14-residue leucine-lysine peptide Ac-LKKLLKLLKKLLKL-NH2 (LKa) is one such amphiphilic peptide. The periodic distribution of hydrophobic and hydrophilic amino acid residues in the sequence of LKa has been shown to promote a-helix formation in an ionic environment and at high peptide concentrations (> ~0.5 mM, no salt). Here, circular dichroism (CD) and nuclear magnetic resonance (NMR) spectroscopy is used to demonstrate that LKa, in the absence of salt and at concentrations

Revised: June 5, 2013 | Published: June 3, 2013

Citation

Buchko G.W., A. Jain, M.L. Reback, and W.J. Shaw. 2013. Structural characterization of the model amphipathic peptide Ac-LKKLLKLLKKLLKL-NH2 in aqueous solution and with 2,2,2-trifluoroethanol and 1,1,1,3,3,3-hexafluoroisopropanol. Canadian Journal of Chemistry 91, no. 6:406-413. PNNL-SA-90953. doi:10.1139/cjc-2012-0429