The folding of a metallopeptide

Ilaria Gamba, Gustavo Rama, Elisabeth Ortega-Carrasco, Roberto Berardozzi, Víctor M. Sánchez-Pedregal, Lorenzo Di Bari, Jean Didier Maréchal, M. Eugenio Vázquez, Miguel Vázquez López

Research output: Contribution to journalArticleResearchpeer-review

7 Citations (Scopus)


© The Royal Society of Chemistry 2016. We have applied solid-phase synthesis methods for the construction of tris(bipyridyl) peptidic ligands that coordinate Fe(ii) ions with high affinity and fold into stable mononuclear metallopeptides. The main factors influencing the folding pathway and chiral control of the peptidic ligands around the metal ions have been studied both by experimental techniques (CD, UV-vis and NMR) and molecular modeling tools. Amongst the numerous molecular variables that have been studied, this study clearly illustrates how the chirality of a given set of aminoacids (proline in this case) of the peptide dictates the chirality of the metal center of the resulting metallopeptide. Moreover, the relatively hydrophobic peptidic models used in this work show that the most stable structures present reduced solvent contacts and, in counterpart, stabilize the cis configuration of the proline residues.
Original languageEnglish
Pages (from-to)881-885
JournalDalton Transactions
Issue number3
Publication statusPublished - 1 Jan 2016


Dive into the research topics of 'The folding of a metallopeptide'. Together they form a unique fingerprint.

Cite this