CRIS Current Research Information System
IRIS è la soluzione IT che facilita la raccolta e la gestione dei dati relativi alle attività e ai prodotti della ricerca. Fornisce a ricercatori, amministratori e valutatori gli strumenti per monitorare i risultati della ricerca, aumentarne la visibilità e allocare in modo efficace le risorse disponibili.
EnglishThe interest in functionalised biomimetic materials used in prosthetic applications as bone substitutes has led to studies on regular alternating polar/non-polar oligopeptides such as EAK-16 (AEAEAKAKAEAEAKAK), first synthesised by Zhang et al. [1]. These peptides have a preferential beta-sheet structure, are resistant to proteolitic cleavage and able to self-assemble into an insoluble macroscopic membrane under physiologial conditions. Their ability to create such stable structures derive from the hydrophobic interaction between the aliphatic groups of non-ionic residues and complementary ionic bonds between acidic and basic amino acids: this stability can be enhanced by the regulation of pH and the presence of monovalent ions. In this context, we studied eight different oligopeptides derived from EAK-16, but modified in their sequence by amino acid substitution or by adding at the N-terminus of the sequence the RGD motif, present in the integrins located in the bone extracellular matrix and able to control osteoblast adhesion.
| Titolo: | Interactions between oligopeptides and oxidised titanium surfaces detected by vibrational spectroscopy. |
| Autore/i: | DI FOGGIA, MICHELE; FAGNANO, CONCEZIO; TADDEI, PAOLA; A. Torreggiani; M. Dettin; TINTI, ANNA |
| Autore/i Unibo: | |
| Anno: | 2009 |
| Titolo del libro: | Book of Abstracts XXI Congresso Nazionale GNSR 2009 |
| Pagina iniziale: | 46 |
| Pagina finale: | 46 |
| Abstract: | The interest in functionalised biomimetic materials used in prosthetic applications as bone substitutes has led to studies on regular alternating polar/non-polar oligopeptides such as EAK-16 (AEAEAKAKAEAEAKAK), first synthesised by Zhang et al. [1]. These peptides have a preferential beta-sheet structure, are resistant to proteolitic cleavage and able to self-assemble into an insoluble macroscopic membrane under physiologial conditions. Their ability to create such stable structures derive from the hydrophobic interaction between the aliphatic groups of non-ionic residues and complementary ionic bonds between acidic and basic amino acids: this stability can be enhanced by the regulation of pH and the presence of monovalent ions. In this context, we studied eight different oligopeptides derived from EAK-16, but modified in their sequence by amino acid substitution or by adding at the N-terminus of the sequence the RGD motif, present in the integrins located in the bone extracellular matrix and able to control osteoblast adhesion. |
| Data prodotto definitivo in UGOV: | 26-feb-2009 |
| Appare nelle tipologie: | 4.02 Riassunto (Abstract) |
File in questo prodotto:
Copyright © 2021