Εξειδίκευση τύπου :	Άρθρο σε επιστημονικό περιοδικό
Τίτλος:	Interactions of the dipeptide paralysin beta-Ala-Tyr and the aminoacid Glu with phospholipid bilayers
Δημιουργός/Συγγραφέας:	Kyrikou, Loanna Benetis, Nikolas P. Chatzigeorgiou, Petros [EL] Ζερβού, Μαρία[EN] Zervou, Maria Viras, Kyriakos Poulos, Constantine [EL] Μαυρομούστακος, Θωμάς[EN] Mavromoustakos, Thomas
Εκδότης:	Elsevier BV
Τόπος έκδοσης:	AMSTERDAM
Ημερομηνία:	2008-01
Γλώσσα:	Αγγλικά
ISSN:	0005-2736
DOI:	10.1016/j.bbamem.2007.09.019
Περίληψη:	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 Ght 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 Ght loaded bilayers. Raman spectroscopy showed that incorporation of Glu in DPPC/watcr 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 Ght 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.
Τίτλος πηγής δημοσίευσης:	Biochimica Et Biophysica Acta (bba) - Biomembranes (formerly Part of Biochimica Et Biophysica Acta (bba) - Biophysics Including Photosynthesis) (incorporating Biochimica Et Biophysica Acta (bba) - Reviews on Biomembranes)
Τόμος/Κεφάλαιο:	1778
Τεύχος:	1
Σελίδες:	113-124
Θεματική Κατηγορία:	[EL] Βιολογία (Γενικά)[EN] Biology (General) [EL] Φυσική[EN] Physics
Λέξεις-Κλειδιά:	paralysin beta-Ala-Tyr C-13 MAS NMR CPP-31NMR broadline differential scanning calorimetry DSC DPPC/water bilayer Raman spectroscopy The aminoacid neurotransmitter Glutamate (L-Glu) Biophysics
Αξιολόγηση από ομότιμους (peer reviewed):	Ναι
Κάτοχος πνευματικών δικαιωμάτων:	© 2007 Elsevier B.V. All rights reserved.
Ηλεκτρονική διεύθυνση περιοδικού (link) :	http://www.elsevier.com/locate/bbamem
ΙΒΦΧΒ: αρχειακή συλλογή:	Ινστιτούτο Οργανικής και Φαρμακευτικής Χημείας (ΙΟΦΧ) (έως 2012)
Εμφανίζεται στις συλλογές:	Ινστιτούτο Χημικής Βιολογίας - Επιστημονικό έργο