http://www.cnr.it/ontology/cnr/individuo/prodotto/ID51205
Vibrational Characterization of Self-Assembling Oligopeptides for Tissue Engineering on TiO2 Surfaces (Articolo in rivista)
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- Label
- Vibrational Characterization of Self-Assembling Oligopeptides for Tissue Engineering on TiO2 Surfaces (Articolo in rivista) (literal)
- Anno
- 2009-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.molstruc.2008.11.004 (literal)
- Alternative label
M. Di Foggia a,* P. Taddei a, C. Fagnano a, A. Torreggiani b, M. Dettin c, S. Sanchez-Cortes d, A. Tinti a (2009)
Vibrational Characterization of Self-Assembling Oligopeptides for Tissue Engineering on TiO2 Surfaces
in Journal of molecular structure (Print)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- M. Di Foggia a,* P. Taddei a, C. Fagnano a, A. Torreggiani b, M. Dettin c, S. Sanchez-Cortes d, A. Tinti a (literal)
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- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- a Dipartimento di Biochimica ''G. Moruzzi\", Sezione di Chimica e Propedeutica Biochimica, Centro di Studio sulla Spettroscopia Raman, Università di Bologna,
Via Belmeloro 8/2, 40126 Bologna, Italy
b ISOF, Consiglio Nazionale delle Ricerche, via P. Gobetti 101, 40129 Bologna, Italy
c Dipartimento di Processi Chimici dell'Ingegneria, Università di Padova, via Marzolo 9, 35131 Padova, Italy
d Istituto de Estructura de la Materia, CSIC, Serrano 121, 28006 Madrid, Spain (literal)
- Titolo
- Vibrational Characterization of Self-Assembling Oligopeptides for Tissue Engineering on TiO2 Surfaces (literal)
- Abstract
- Four alternating polar/non-polar peptides derived from the self-assembling peptide EAK-16 (Ac-AEAKAEAKAEAKAEAK-
NH2) were examined in comparison with the EAK-16 parent form (peptide 1), both
as-synthesised and after deposition on TiO2. The peptides were studied for their possible use as biomimetic
materials due to their auto-assembling properties and to the presence, in two of them, of the
RGD sequence, an active modulator of cell adhesion.
IR and Raman spectroscopies were used to investigate the influence of the amino acid substitutions in
the sequence on the self-assembly before and after deposition on TiO2. SERS spectroscopy was also used
to elucidate the interaction with metal. As regards the as-synthesised peptides, basic amino acid substitution
(K?O, peptide 2) or contemporaneous acid and basic substitution (E?D and K?O, peptide 3)
did not induce significant conformational changes with respect to peptide 1: the prevailing structure was
beta-sheet (about 70%). The insertion of the RGD sequence (peptide 4), induced a decrease in beta-sheet
content (50%); the simultaneous scrambling of the sequence (peptide 5) made alfa-helix the prevailing
structure.
After deposition on TiO2 all peptides showed that the interaction with the surface was mediated by carboxylate
groups; peptides maintained a prevalent beta-sheet structure with slightly higher percentages
for peptides 1 and 4 which proved to form a more ordered layer. In conclusion, the substitution of polar
aminoacid residues influences the ability of self-assembling more than the insertion of the RGD sequence,
while the scrambling of the sequence did not appreciably alter the peptide ability of self-assembling on
TiO2. (literal)
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