Role of tryptophan-14 in the interaction of dynorphin A(1-17) with micelles.
Fluorescence spectroscopy has been used to examine the interaction between the opioid peptide dynorphin A(1-17) (dynorphin) and dodecylphosphocholine (DPC) micelles. Fluorescence emission spectra as a function of added lipid indicate insertion of the Trp14 side chain into the hydrophobic portion of the micelle, supporting NMR results from this laboratory. A model of interaction with micelles consistent with the fluorescence results and earlier NMR results is proposed. The critical micelle concentration in the presence of peptide was also determined, and is discussed in the context of relevance to both NMR spectroscopy and peptide-lipid interactions.
Tessmer
M R
MR
Department of Medicinal Chemistry, University of Minnesota, Minneapolis, USA.
Kallick
D A
DA
D000595:Amino Acid Sequence; D001665:Binding Sites; D004399:Dynorphins / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008823:Micelles; D008961:Models, Structural; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D010767:Phosphorylcholine / Q000031:analogs & derivatives* / Q000737:chemistry; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D014364:Tryptophan
D008823:Micelles; D010767:Phosphorylcholine; C028810:dodecylphosphocholine; D004399:Dynorphins; D014364:Tryptophan