Interactions of the dipeptide paralysin beta-Ala-Tyr and the aminoacid Glu with phospholipid bilayers.
Existing evidence points out that the biological activity of beta-Ala-Tyr may in part related to its interactions with the cell membranes. For comparative reasons the effects of Glu were also examined using identical techniques and conditions. In order to examine their thermal and dynamic effects on membrane bilayers a combination of DSC, Raman and solid state NMR spectroscopy on DPPC/water model membranes were applied and the results were compared. DSC data showed that Glu perturbs to a greater degree the model membrane compared to beta-Ala-Tyr. Thus, alteration of the phase transition temperature and half width of the peaks, abolishment of the pretransition and influence on the enthalpy of the phase transition were more pronounced in the Glu loaded bilayers. Raman spectroscopy showed that incorporation of Glu in DPPC/water bilayers increased the order in the bilayers in contrast to the effect of the dipeptide. Several structural and dynamical properties of the DPPC multilamellar bilayers with and without the dipeptide or Glu were compared using high resolution C-13 MAS (Magic Angle Spinning) spectra and spectral simulations of inhomogeneously broadened, stationary P-31 NMR lineshapes measured under CP (Cross-polarization) conditions. These methods revealed that the aminoacid Glu binds in the close realm of the phosphate in the hydrophilic headgroup of DPPC while beta-Ala-Tyr is located more deeply inside the hydrophobic zone of the bilayer. The P-31 NMR simulations indicated restricted fast rotary motion of the phospholipids about their long axes in the organized bilayer structure. Finally, by the applied methodologies it is concluded that the two molecules under study exert dissimilar thermal and dynamic effects on lipid bilayers, the Glu improving significantly the packing of the lipids in contrast to the smaller and opposite effect of the dipeptide.
Kyrikou
Ioanna
I
Institute of Organic and Pharmaceutical Chemistry, National Hellenic Research Foundation, Vas. Constantinou 48, Athens 11635, Greece.
Benetis
Nikolas P
NP
Chatzigeorgiou
Petros
P
Zervou
Maria
M
Viras
Kyriakos
K
Poulos
Constantine
C
Mavromoustakos
Thomas
T
D015060:1,2-Dipalmitoylphosphatidylcholine / Q000737:chemistry / Q000378:metabolism*; D002152:Calorimetry, Differential Scanning; D002247:Carbon Isotopes; D003198:Computer Simulation; D004151:Dipeptides / Q000737:chemistry / Q000378:metabolism*; D018698:Glutamic Acid / Q000737:chemistry / Q000378:metabolism*; D008051:Lipid Bilayers / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D044367:Phase Transition; D013059:Spectrum Analysis, Raman; D013696:Temperature
D002247:Carbon Isotopes; D004151:Dipeptides; D008051:Lipid Bilayers; D015060:1,2-Dipalmitoylphosphatidylcholine; C016968:alanyltyrosine; D018698:Glutamic Acid