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Apolipoprotein A‐I peptide models as probes to formulate potential inhibitors of the low‐density lipoprotein oxidation
Author(s) -
Darvari Maria I.,
Petraki Maria P.,
Tellis Constantinos,
Harilogis Konstantinos,
Tselepis Alexandros D.,
SakarellosDaitsiotis Maria
Publication year - 2011
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.1391
Subject(s) - peptide , chemistry , lipoprotein , scavenger receptor , apolipoprotein b , biochemistry , helix (gastropod) , low density lipoprotein , scavenger , stereochemistry , biophysics , cholesterol , antioxidant , biology , ecology , snail
Apolipoprotein A‐I (apoA‐I), which constitutes the principal protein component of high‐density lipoprotein, is responsible for its major antiatherogenic functions. Aiming at contributing to the development of potent inhibitors of low‐density lipoprotein (LDL) peptide models of helices 4,6 and 9,10 of apoA‐I were designed and synthesized. Specific amino acid substitutions, resulting in transformation of the original helix class A and Y to G according to the Schiffer and Edmundson helical wheel representation, were introduced in order to validate the contribution of these modifications in the inhibitory activity of the synthesized peptide models against the LDL oxidation. The role of Met at positions 112 (helix 4) and 148 (helix 6) as oxidant scavenger was also investigated. The helical characteristics of all the peptide models were studied by CD in membrane‐mimicking microenvironments and compared with the original helices. Copyright © 2011 European Peptide Society and John Wiley & Sons, Ltd.