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Issue 3, 2016
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The folding of a metallopeptide

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Abstract

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.

Graphical abstract: The folding of a metallopeptide

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Publication details

The article was received on 22 Jul 2015, accepted on 25 Oct 2015 and first published on 27 Oct 2015


Article type: Communication
DOI: 10.1039/C5DT02797G
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Dalton Trans., 2016,45, 881-885

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    The folding of a metallopeptide

    I. Gamba, G. Rama, E. Ortega-Carrasco, R. Berardozzi, V. M. Sánchez-Pedregal, L. Di Bari, J. Maréchal, M. E. Vázquez and M. Vázquez López, Dalton Trans., 2016, 45, 881
    DOI: 10.1039/C5DT02797G

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