Institut des Sciences Moléculaires d'Orsay




vendredi 21 février

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Accueil > Équipes scientifiques > Structure et dynamique des systèmes complexes isolés photoexcités (SYSIPHE) > CHIralité et spectroscoPIE (CHIPIE) > Influence of residue’s chirality on the structure of polypetides

Influence of residue’s chirality on the structure of polypetides

The structure of biopolymers like peptides or proteins depend on many factors, among them the environment, the nature of the building blocks they are made from, and their chirality. We have undertaken the study of di and tetrapetides built from phenylalanine to assess the influence of the chirality of the residue on the structure of the molecule .

Ion mobility experiments are combined with Infra-Red Multiple Photon Dissociation (IRMPD) spectroscopy and quantum chemical calculations for assessing the role of chirality in the structure of protonated and sodiated di- or tetra-peptides. Sodiated systems show a strong chirality dependence of the competition between Na+…O and Na+…π interactions. Chirality effects are more subtle in protonated systems and manifest themselves by differences in the secondary interactions such hydrogen bonds between neutral groups or those involving the aromatic rings.

This collaborative work also involves Debora Scuderi from Laboratoire de Chimie Physique (LCP) and laser à électrons libres CLIO for IRMPD experiments, Fabien Chirot from Institut des Sciences Analytiques in Lyon and Philippe Dugourd from Institut Laser Matière in Lyon for ion mobility experiments, and Carine Clavaguera for quantum chemical calculations.

Chirality-dependent structuration of protonated or sodiated polyphenylalanines : IRMPD and ion mobility studies
Valeria Lepere, Katia Le Barbu-Debus, Carine Clavaguéra, Debora Scuderi,
Giovanni Piani, Anne-Laure Simon, Fabien Chirot, Luke MacAleese,
Philippe Dugourd and Anne Zehnacker
Phys. Chem. Chem. Phys, 2016, 18, 1807–1817