Philippe Minard

Marie Valerio-Lepiniec6
Agathe Urvoas4
6Marie Valerio-Lepiniec
4Agathe Urvoas
Learn More
Long insertions into a loop of a folded host protein are expected to have destabilizing effects because of the entropic cost associated with loop closure unless the inserted sequence adopts a folded structure with amino- and carboxy-termini in close proximity. A loop entropy reduction screen based on this concept was used in an attempt to retrieve folded(More)
  • Anne Chevrel, Agathe Urvoas, Ines Li de la Sierra-Gallay, Magali Aumont-Nicaise, Sandrine Moutel, Michel Desmadril +5 others
  • 2015
A family of artificial proteins, named αRep, based on a natural family of helical repeat was previously designed. αRep members are efficiently expressed, folded and extremely stable proteins. A large αRep library was constructed creating proteins with a randomized interaction surface. In the present study, we show that the αRep library is an efficient(More)
Ankyrins are cellular repeat proteins, which can be genetically modified to randomize amino-acid residues located at defined positions in each repeat unit, and thus create a potential binding surface adaptable to macromolecular ligands. From a phage-display library of artificial ankyrins, we have isolated Ank(GAG)1D4, a trimodular ankyrin which binds to the(More)
Specific, tight-binding protein partners are valuable helpers to facilitate membrane protein (MP) crystallization, because they can i) stabilize the protein, ii) reduce its conformational heterogeneity, and iii) increase the polar surface from which well-ordered crystals can grow. The design and production of a new family of synthetic scaffolds (dubbed(More)
Ankyrins are cellular mediators of a number of essential protein-protein interactions. Unlike intrabodies, ankyrins are composed of highly structured repeat modules characterized by disulfide bridge-independent folding. Artificial ankyrin molecules, designed to target viral components, might act as intracellular antiviral agents and contribute to the(More)
  • Maximiliano Figueroa, Julie Vandenameele, Erik Goormaghtigh, Marie Valerio-Lepiniec, Philippe Minard, André Matagne +1 other
  • 2016
The artificial protein Octarellin V.1 ([1]) was obtained through a direct evolution process over the de novo designed Octarellin V ([2]). The protein has been characterized by circular dichroism and fluorescence techniques, in order to obtain data related to its thermo(More)
  • Asma Guellouz, Marie Valerio-Lepiniec, Agathe Urvoas, Anne Chevrel, Marc Graille, Zaineb Fourati-Kammoun +3 others
  • 2013
We previously designed a new family of artificial proteins named αRep based on a subgroup of thermostable helicoidal HEAT-like repeats. We have now assembled a large optimized αRep library. In this library, the side chains at each variable position are not fully randomized but instead encoded by a distribution of codons based on the natural frequency of(More)
  • 1