Conformational study of new amphipathic alpha-helical peptide models of apoA-I as potential atheroprotective agents
Φόρτωση...
Ημερομηνία
Συγγραφείς
Beaufils, C.
Alexopoulos, C.
Petraki, M. P.
Tselepis, A. D.
Coudevylle, N.
Sakarellos-Daitsiotis, M.
Sakarellos, C.
Cung, M. T.
Τίτλος Εφημερίδας
Περιοδικό ISSN
Τίτλος τόμου
Εκδότης
Wiley
Περίληψη
Τύπος
Είδος δημοσίευσης σε συνέδριο
Είδος περιοδικού
peer reviewed
Είδος εκπαιδευτικού υλικού
Όνομα συνεδρίου
Όνομα περιοδικού
Biopolymers
Όνομα βιβλίου
Σειρά βιβλίου
Έκδοση βιβλίου
Συμπληρωματικός/δευτερεύων τίτλος
Περιγραφή
Aiming at contributing to the development of potential atheroprotective,agents, we report on the concept and design of two peptide models, which mimic the amphipathic helices of apoA-I and incorporate Met into their sequences to validate its role as oxidant scavenger. Ac-ESK(Palm)(KELSKSWSEMLKEK)-S-10-L-13(Palm)SKS-NH2 (model 1 [W-10, M-13]) and Ac-ESK(Palm)(KELSKSMSEW13)-S-10 LKEK(Palm)SKS-NH2 (model 2 [M-10 W-13]). Hydrophobic residues of both models cover about the half of the surface, while the positively and negatively charged residues constitute two separate clusters on the hydrophilic face. Palmitoyl groups were introduced into the Lys-(MH2)-H-s groups at positions 3 and 17 to contribute to the amphipathic character of the peptides and stabilize the nonpolar face of the helix. Conformational study by the combined application of 2D-NMR and molecular dynamics simulations, CD, FTIR, and fluorescence spectroscopy revealed that model I adopts helical conformation and Met is well exposed to the microenvironment. Model 2 that derives from model 1 by exchanging W-10 (model 1) with M-10 and M-13 (model 1) with W-13 also displays helical characteristics, while Met is rather shielded. Oxidation experiments indicated that model I exhibits a 2-fold more potent antioxidant activity towards LDL oxidation, compared to model 2, confirming the role of Met, when is devoid of steric hindrances, as oxidant scavenger for the protection of LDL. (c) 2006 Wiley Periodicals, Inc.
Περιγραφή
Λέξεις-κλειδιά
apolipoprotein a-i, amphipathic alpha-helix, atheroprotective peptide models, hdl, ldl, 2d-nmr, noesy, molecular modeling, cd, fluorescence, apolipoprotein-a-i, magnetic-resonance spectroscopy, low-density-lipoprotein, solid-phase synthesis, 3-dimensional structures, oxidative modification, structural-analysis, secondary structure, cholesterol efflux, nmr-spectroscopy
Θεματική κατηγορία
Παραπομπή
Σύνδεσμος
<Go to ISI>://000245937400004
http://onlinelibrary.wiley.com/store/10.1002/bip.20651/asset/20651_ftp.pdf?v=1&t=h0e0j28c&s=9fbd1743dff12c6027f907bf0a89436d47b8c4e8
http://onlinelibrary.wiley.com/store/10.1002/bip.20651/asset/20651_ftp.pdf?v=1&t=h0e0j28c&s=9fbd1743dff12c6027f907bf0a89436d47b8c4e8
Γλώσσα
en
Εκδίδον τμήμα/τομέας
Όνομα επιβλέποντος
Εξεταστική επιτροπή
Γενική Περιγραφή / Σχόλια
Ίδρυμα και Σχολή/Τμήμα του υποβάλλοντος
Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας