Interactions between peptides are relevant from a biomedical point of view, in particular for the role played by their aggregates in different important pathologies, and also because peptide aggregates represent promising scaffolds for innovative materials. In the present article, the aggregation properties of the homo-peptides formed by α-aminoisobutyric acid (U) residues are discussed. The peptides investigated have chain lengths between six and 15 residues and comprise benzyl and naphthyl groups at the N- and C-termini, respectively. Spectroscopic experiments and molecular dynamics simulations show that the shortest homopeptide, constituted by six U, does not exhibit any tendency to aggregate under the conditions examined. On the other hand, the homologous peptide with 15 U forms very stable and compact aggregates in 70/30(v/v) methanol/water solution. Atomic force microscopy images indicate that these aggregates promote formation of long fibrils once they are deposited on a mica surface. The aggregation phenomenon is mainly due to hydrophobic interactions occurring between very stable helical structures, and the aromatic groups in the peptides seem to play a minor role.

Bocchinfuso, G., Conflitti, P., Raniolo, S., Caruso, M., Mazzuca, C., Gatto, E., et al. (2014). Aggregation propensity of Aib homo-peptides of different length: an insight from molecular dynamics simulations. JOURNAL OF PEPTIDE SCIENCE, 20, 494-507 [10.1002/psc.2648].

Aggregation propensity of Aib homo-peptides of different length: an insight from molecular dynamics simulations

BOCCHINFUSO, GIANFRANCO;MAZZUCA, CLAUDIA;GATTO, EMANUELA;VENANZI, MARIANO;PALLESCHI, ANTONIO
2014

Abstract

Interactions between peptides are relevant from a biomedical point of view, in particular for the role played by their aggregates in different important pathologies, and also because peptide aggregates represent promising scaffolds for innovative materials. In the present article, the aggregation properties of the homo-peptides formed by α-aminoisobutyric acid (U) residues are discussed. The peptides investigated have chain lengths between six and 15 residues and comprise benzyl and naphthyl groups at the N- and C-termini, respectively. Spectroscopic experiments and molecular dynamics simulations show that the shortest homopeptide, constituted by six U, does not exhibit any tendency to aggregate under the conditions examined. On the other hand, the homologous peptide with 15 U forms very stable and compact aggregates in 70/30(v/v) methanol/water solution. Atomic force microscopy images indicate that these aggregates promote formation of long fibrils once they are deposited on a mica surface. The aggregation phenomenon is mainly due to hydrophobic interactions occurring between very stable helical structures, and the aromatic groups in the peptides seem to play a minor role.
Pubblicato
Rilevanza internazionale
Articolo
Esperti anonimi
Settore CHIM/02 - Chimica Fisica
English
Con Impact Factor ISI
α-aminoisobutyric acid; helical fibrils; inversion helical chirality; conformational studies; spectroscopy; atomic force microscopy; role of aromatics; peptide self-aggregation
Bocchinfuso, G., Conflitti, P., Raniolo, S., Caruso, M., Mazzuca, C., Gatto, E., et al. (2014). Aggregation propensity of Aib homo-peptides of different length: an insight from molecular dynamics simulations. JOURNAL OF PEPTIDE SCIENCE, 20, 494-507 [10.1002/psc.2648].
Bocchinfuso, G; Conflitti, P; Raniolo, S; Caruso, M; Mazzuca, C; Gatto, E; Placidi, E; Formaggio, F; Toniolo, C; Venanzi, M; Palleschi, A
Articolo su rivista
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/2108/103952
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 14
  • ???jsp.display-item.citation.isi??? 14
social impact