Margot Lefèvre
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Research Interests
Margot Lefèvre has a total of 3 co-authors. Here are the top co-authors by number of shared publications:
- Charlène Esmieu
LCC-CNRS Université de Toulouse CNRS 31400 Toulouse France
1 shared publication - Christelle Hureau
Univ Toulouse, CNRS, LCC, Toulouse, France
1 shared publication - Kyangwi Patrick Malikidogo
Univ. Grenoble Alpes, CNRS, CEA, IRIG, LCBM (UMR 5249), F-38000 Grenoble, France
1 shared publication
Latest Publications
- Open Access
Sequence–Activity Relationship of ATCUN Peptides in the Context of Alzheimer’s Disease
Amino-terminal CuII and NiII (ATCUN) binding sequences are widespread in the biological world. Here, we report on the study of eight ATCUN peptides aimed at targeting copper ions and stopping the associated formation of reactive oxygen species (ROS). This study was actually more focused on Cu(Aβ)-induced ROS production in which the Aβ peptide is the “villain” linked to Alzheimer’s disease. The full characterization of CuII binding to the ATCUN peptides, the CuII extraction from CuII(Aβ), and the ability of the peptides to prevent and/or stop ROS formation are described in the relevant biological conditions. We highlighted in this research that all the ATCUN motifs studied formed the same thermodynamic complex but that the addition of a second histidine in position 1 or 2 allowed for an improvement in the CuII uptake kinetics. This kinetic rate was directly related to the ability of the peptide to stop the CuII(Aβ)-induced production of ROS, with the most efficient motifs being HWHG and HGHW.
Open AccessSequence–Activity Relationship of ATCUN Peptides in the Context of Alzheimer’s Disease
Amino-terminal CuII and NiII (ATCUN) binding sequences are widespread in the biological world. Here, we report on the study of eight ATCUN peptides aimed at targeting copper ions and stopping the associated formation of reactive oxygen species (ROS). This study was actually more focused on Cu(Aβ)-induced ROS production in which the Aβ peptide is the “villain” linked to Alzheimer’s disease. The full characterization of CuII binding to the ATCUN peptides, the CuII extraction from CuII(Aβ), and the ability of the peptides to prevent and/or stop ROS formation are described in the relevant biological conditions. We highlighted in this research that all the ATCUN motifs studied formed the same thermodynamic complex but that the addition of a second histidine in position 1 or 2 allowed for an improvement in the CuII uptake kinetics. This kinetic rate was directly related to the ability of the peptide to stop the CuII(Aβ)-induced production of ROS, with the most efficient motifs being HWHG and HGHW.