Conformational analysis of novel heparin binding peptides (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• Conformational analysis of novel heparin binding peptides (Articolo in rivista) (literal)

Anno

• 2005-01-01T00:00:00+01:00 (literal)

Alternative label

• M. Vacatello, G. D’ Auria, L. Falcigno, M. Dettin, R. Gambaretto, C. Di Bello & L. Paolillo (2005)
  Conformational analysis of novel heparin binding peptides
  in Biomaterials
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• M. Vacatello, G. D’ Auria, L. Falcigno, M. Dettin, R. Gambaretto, C. Di Bello & L. Paolillo (literal)

Pagina inizio

• 3207 (literal)

Pagina fine

• 3214 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 26 (literal)

Rivista

• Biomaterials (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#descrizioneSinteticaDelProdotto

• Pubblicazione su rivista scientifica (literal)

Note

• ISI Web of Science (WOS) (literal)

Titolo

• Conformational analysis of novel heparin binding peptides (literal)

Abstract

• A properly engineered biomaterial for dental/orthopedic applications must induce specific responses from the osteoblasts at the implant site. A most desirable response is an efficient adhesion, as it represents the first phase in the cell/material interaction and the quality of this phase will influence the cell's capacity to organize into a new functional tissue. The four osteoblast-adhesive peptides discussed in this paper are mapped on the 339-364 sequence (339MAPRPSLAKKQRFRHRNRKGYRSQRG364) located in the primary heparin-binding site of human vitronectin (HVP). Adsorbed on a polystyrene scaffold, these peptides display different adhesive activities towards osteoblasts. In this paper we report on the structural anal. in soln. of the peptides through NMR and computational techniques. We find that the peptides with the highest adhesive activities display a hydrophobic patch opposite to the charged surface candidate to interact with heparin. These findings suggest that the peptides might adsorb on the polystyrene support in a favorable orientation for their activity. Furthermore, mol. models obtained for the four peptides in soln. were used in rigid docking simulations with a heparin model. Assuming that the peptide soln. conformations are not very different from the polystyrene-adsorbed structures, the simulations reveal that peptide adhesive activity is also affected by the no. of ionic interactions and spacing between charged residues (literal)

Prodotto di

• Sviluppo di repertori molecolari per l'identificazione di antagonisti di interazioni proteina-proteina e proteina-ligando (PM.P01.005.001) (Modulo)
• Institute of biostructure and bioimaging (IBB) (Istituto)

Autore CNR

• LUCIA FALCIGNO (Unità di personale esterno)

Insieme di parole chiave

• Keywords of "Conformational analysis of novel heparin binding peptides" (Insieme di parole chiave)

Incoming links:

Prodotto

• Institute of biostructure and bioimaging (IBB) (Istituto)
• Sviluppo di repertori molecolari per l'identificazione di antagonisti di interazioni proteina-proteina e proteina-ligando (PM.P01.005.001) (Modulo)

Autore CNR di

• LUCIA FALCIGNO (Unità di personale esterno)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Biomaterials (Rivista)

Insieme di parole chiave di

• Keywords of "Conformational analysis of novel heparin binding peptides" (Insieme di parole chiave)