http://www.cnr.it/ontology/cnr/individuo/prodotto/ID14138

Structural Analysis of a Helical Peptide Unfolding Pathway (Articolo in rivista)

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Structural Analysis of a Helical Peptide Unfolding Pathway (Articolo in rivista) (literal)

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Diana D, Ziaco B, Scarabelli G, Pedone C, Colombo G, D'Andrea LD, Fattorusso R (2010)
Structural Analysis of a Helical Peptide Unfolding Pathway
in Chemistry - A European Journal
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Diana D, Ziaco B, Scarabelli G, Pedone C, Colombo G, D'Andrea LD, Fattorusso R (literal)

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Diana D, CNR, Ist Biostrutture & Bioimmagini, I-80134 Naples, Italy; Ziaco B, CNR, Ist Biostrutture & Bioimmagini, I-80134 Naples, Italy; Scarabelli G, CNR, Ist Chim Riconoscimento Mol, I-20131 Milan, Italy; Pedone C, Univ Naples Federico 2, Dipartimento Sci Biol, I-80134 Naples, Italy; Colombo G, CNR, Ist Chim Riconoscimento Mol, I-20131 Milan, Italy; D'Andrea LD, CNR, Ist Biostrutture & Bioimmagini, I-80134 Naples, Italy; Fattorusso R, Univ Naples 2, Dipartimento Sci Ambientali, I-81100 Caserta, Italy; (literal)

Titolo

Abstract

The analysis of the folding mechanism in peptides adopting well-defined secondary structure is fundamental to understand protein folding. Herein, we describe the thermal unfolding of a 1.5-mer vascular endothelial growth factor mimicking a-helical peptide (QK(L10A)) through the combination of spectroscopic and computational analyses. In particular, on the basis of the temperature dependencies of QK(L10A) H(alpha) chemical shifts we show that the first phase of the thermal helix unfolding, ending at around 320 K, involves mainly the terminal regions. A second phase of the transition, ending at around 333 K, comprises the central helical region of the peptide. The determination of high-resolution QK(L10A) conformational preferences in water at 313 K allowed us to identify, at atomic resolution, one intermediate of the folding unfolding pathway. Molecular dynamics simulations corroborate experimental observations detecting a stable central helical turn, which represents the most probable site for the helix nucleation in the folding direction. The data presented herein allows us to draw a folding unfolding picture for the small peptide QK(L10A) compatible with the nucleation-propagation model. This study, besides contributing to the basic field of peptide helix folding, is useful to gain an insight into the design of stable helical peptides, which could find applications as molecular scaffolds to target protein-protein interactions. (literal)

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