Anti-inflammatory activity of superoxide dismutase mimics functionalized with cell-penetrating peptides
Author(s) -
Émilie Mathieu,
Anne-Sophie Bernard,
H. Y. Vincent Ching,
Andréa Somogyi,
Kadda Medjoubi,
Jennifer Rodon Fores,
Hélène Bertrand,
Amandine Vincent,
Sylvain Trépout,
JeanLuc GuerquinKern,
Andreas Scheitler,
Ivana IvanovićBurmazović,
Philippe Seksik,
Nicolas Delsuc,
Clotilde Policar
Publication year - 2020
Publication title -
dalton transactions
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.98
H-Index - 184
eISSN - 1477-9234
pISSN - 1477-9226
DOI - 10.1039/c9dt04619d
Subject(s) - superoxide dismutase , moiety , chemistry , anti inflammatory , superoxide , enzyme , dismutase , biophysics , biochemistry , cell , stereochemistry , pharmacology , biology
A superoxide dismutase mimic (Mn1) was functionalized with three positively charged-peptides: (Mn1-R9), RRWWWRRWRR (Mn1-RW9) or F x -r-F x -K (Mn1-MPP). Characterization of the physico-chemical properties of the complexes show that they share similar binding affinity for Mn 2+ , apparent reduction potential and intrinsic superoxide dismutase activity. However, their accumulation in cells is different (Mn1-R9 < Mn1-MPP < Mn1-RW9 < Mn1), as well as their subcellular distribution. In addition, the three functionalized-complexes display a better anti-inflammatory activity than Mn1 when assayed at 10 μM. This improvement is due to a combination of an anti-inflammatory effect of the peptidyl moiety itself, and of the SOD mimic for Mn1-RW9 and Mn1-MPP. In contrast, the enhanced anti-inflammatory activity of Mn1-R9 is solely due to the SOD mimic.
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