Conformational disorder in phosphopeptides: solution studies by CD and NMR techniques

• Authors: Marilisa Leone , Flavia Anna Mercurio , Marian Vincenzi , Antonella Accardo , Paola Ringhieri , Diego Tesauro , Frédéric Carrière , Filomena Rossi
• Languages of publication: EN

Abstracts

EN

In the last few years intrinsically disordered proteins (IDPs) have received great attention from the scientific community as they participate in several important biological processes and diseases. The intrinsic disorder and flexibility of IDPs grant them a number of advantages with respect to ordered proteins, such as conformational plasticity to bind several targets, a large interaction surface, involvement in high specificity/low affinity interactions, enhanced binding kinetics. It is assumed that post-translational modifications such as phosphorylation can stimulate structural rearrangement in IDPs and facilitate their binding to partners. To better understand at a structural level the multifaceted mechanisms that govern molecular recognition processes involving IDPs, we designed, synthesized by solid phase methods, and structurally characterized unstructured peptides. These molecules contain a putative disordered module, flanked at either the N- or C-terminal ends by a different phosphorylated amino acid (serine or threonine) to mimick the effects of phosphorylation. The absence of an ordered state in the designed peptides was proved experimentally by CD and NMR conformational studies that were carried out under different solution conditions

Keywords

EN

intrinsically disordered peptides; peptide design; Solid Phase Peptide Synthesis (SPPS); Circular Dichroism (CD); Nuclear Magnetic Resonance Spectroscopy (NMR)

• Publisher: De Gruyter Open
• Journal: Peptidomics
• Year: 2014
• Volume: 1
• Issue: 1

Dates

published

1 - 1 - 2014

online

2 - 7 - 2014

Contributors

author

Marilisa Leone

• Institute of Biostructures and Bioimaging (IBB-CNR), Via Mezzocannone 16, 80134 Naples, Italy / Centro Interuniversitario di Ricerca sui Peptidi Bioattivi (CIRPEB), Via Mezzocannone 16, 80134 Naples, Italy

author

Flavia Anna Mercurio

• Institute of Biostructures and Bioimaging (IBB-CNR), Via Mezzocannone 16, 80134 Naples, Italy

author

Marian Vincenzi

• University of Naples “Federico II”, Department of Pharmacy, Via Mezzocannone 16, 80134 Naples, Italy

author

Antonella Accardo

• Institute of Biostructures and Bioimaging (IBB-CNR), Via Mezzocannone 16, 80134 Naples, Italy / Centro Interuniversitario di Ricerca sui Peptidi Bioattivi (CIRPEB), Via Mezzocannone 16, 80134 Naples, Italy/ University of Naples “Federico II”, Department of Pharmacy, Via Mezzocannone 16, 80134 Naples, Italy

author

Paola Ringhieri

• Centro Interuniversitario di Ricerca sui Peptidi Bioattivi (CIRPEB), Via Mezzocannone 16, 80134 Naples, Italy/ University of Naples “Federico II”, Department of Pharmacy, Via Mezzocannone 16, 80134 Naples, Italy

author

Diego Tesauro

• Institute of Biostructures and Bioimaging (IBB-CNR), Via Mezzocannone 16, 80134 Naples, Italy / Centro Interuniversitario di Ricerca sui Peptidi Bioattivi (CIRPEB), Via Mezzocannone 16, 80134 Naples, Italy/ University of Naples “Federico II”, Department of Pharmacy, Via Mezzocannone 16, 80134 Naples, Italy

author

Frédéric Carrière

• CNRS - Aix-Marseille Université - Enzymologie Interfaciale et Physiologie de la Lipolyse - UMR 7282, 31 chemin Joseph Aiguier, 13402 Marseille cedex 20, France

author

Filomena Rossi

• Institute of Biostructures and Bioimaging (IBB-CNR), Via Mezzocannone 16, 80134 Naples, Italy/ Centro Interuniversitario di Ricerca sui Peptidi Bioattivi (CIRPEB), Via Mezzocannone 16, 80134 Naples, Italy/ University of Naples “Federico II”, Department of Pharmacy, Via Mezzocannone 16, 80134 Naples, Italy

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Identifiers

DOI

10.2478/ped-2014-0001