Olga Iranzo

Affiliation: Institut des Sciences Moléculaires de Marseille, UMR 7313, Aix Marseille Université CNRS, Marseille


Research interests: Metallopeptides, peptidomimetics

Fine-tuning the Structure of His-containing Peptides for Copper Binding
Ana Fragoso,a Tiago Carvalho,c Pedro Lamosa,a Rita Delgadoa , Daniela Valensinb and Olga Iranzoa,c
a) Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, 2780-157 Oeiras, Portugal
b) Department of Biotechnology, Chemistry and Pharmacy, University of Siena, 53100 Siena, Italy
c) Aix Marseille Université, Centrale Marseille, CNRS, iSm2 UMR 7313, 13397 Marseille, France, olga.iranzo@univ-amu.fr

Designing small peptides capable of binding Cu(II) mainly by the side chain functionalities and forming single species in the neutral pH range is a hard task since the amide nitrogens strongly compete for Cu(II) coordination [1]. However, metalloproteins are proficient on this and generate the appropriated coordination pocket to avoid amide coordination. This exquisite control allows copper proteins to attain a myriad of catalytic activities and thus, a large variety of biological functions [2]. Achieving this with short peptides will be very appealing to engineer miniaturized copper proteins with potential redox and hydrolytic activities.

Recently, we have designed two His-containing decapeptides, a cyclic (C-Asp) and an open derivative (O-Asp), capable of coordinating Cu(II) [3]. Potentiometric, mass spectrometric and spectroscopic studies indicate that at 1:1 Cu(II)/peptide ratio these peptides form similar single Cu(II) species at close to neutral pH values and that Cu(II) is exclusively coordinated by the side chain functionalities [3,4]. Interestingly, different redox properties were observed for these similar species due to the distinct intrinsic nature of their peptidic scaffolds. Possible consequences of all these findings in catalysis will be discussed.

 

References.

1. a) Sigel H; Martin R. B. Chem. Rev. 1982, 82, 385-426. b) Kozłowski H.; Bal W.; Dyba M.; Kowalik-Jankowska T. Coord. Chem. Rev. 1999, 184, 319-346.

2. a) Holm R. H.; Kennepohl P.; Solomon E. I. Chem. Rev. 1996, 96, 2239-2314; b) Gaggelli E.; Kozłowski H.; Valensin D.; Valensin G.; Chem. Rev. 2006, 106, 1995-2044.

3. Fragoso A.; Lamosa P.; Delgado R.; Iranzo O. Chem. Eur. J., 2013, 19, 2076-2088.

4. Fragoso A.; Delgado R.; Iranzo O. Dalton Trans., 2013, 42, 6182-6192.