RT Journal Article
T1 The folding of a metallopeptide
A1 Gamba, Ilaria
A1 Rama, Gustavo
A1 Ortega-Carrasco, Elisabeth
A1 Berardozzi, Roberto
A1 Sánchez Pedregal, Víctor Manuel
A1 Di Bari, Lorenzo
A1 Maréchal, Jean-Didier
A1 Vázquez Sentís, Marco Eugenio
A1 Vázquez López, Miguel
AB 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
PB Royal Society of Chemistry
SN 1477-9226
YR 2016
FD 2016
LK http://hdl.handle.net/10347/17022
UL http://hdl.handle.net/10347/17022
LA eng
NO Gamba, I., Rama, G., Ortega-Carrasco, E., Berardozzi, R., Sánchez-Pedregal, V., & Di Bari, L. et al. (2016). The folding of a metallopeptide. Dalton Transactions, 45(3), 881-885. doi: 10.1039/c5dt02797g
NO We are thankful for the support given by the Spanish grantsSAF2013-41943-R, CTQ2012-31341, CTQ2011-23336 andCTQ2013-49317-EXP; the ERDF and the European ResearchCouncil (Advanced Grant 340055); the Xunta de Galicia grantsGRC2013-041 and PGIDIT08CSA-047209PR and the Generalitatde Catalunya grant 2009SGR68. Support of COST ActionCM1105 is kindly acknowledged. G.R. thanks the INL for hisPhD fellowship
DS Minerva
RD 28 abr 2026