http://www.cnr.it/ontology/cnr/individuo/prodotto/ID190352
C-terminal truncation of Vascular Endothelial Growth Factor mimetic helical peptide preserves structural and receptor binding properties (Articolo in rivista)
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- Label
- C-terminal truncation of Vascular Endothelial Growth Factor mimetic helical peptide preserves structural and receptor binding properties (Articolo in rivista) (literal)
- Anno
- 2012-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.bbrc.2012.06.109 (literal)
- Alternative label
Ziaco B, Diana D, Capasso D, Palumbo R, Celentano V, Di Stasi R, Fattorusso R, D'Andrea LD (2012)
C-terminal truncation of Vascular Endothelial Growth Factor mimetic helical peptide preserves structural and receptor binding properties
in Biochemical and biophysical research communications (Print)
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Ziaco B, Diana D, Capasso D, Palumbo R, Celentano V, Di Stasi R, Fattorusso R, D'Andrea LD (literal)
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- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- 1. CNR, Ist Biostrutture & Bioimmagini, I-80134 Naples, Italy
2. Univ Naples Federico II, Fac Sci Biotecnol, I-80134 Naples, Italy
3. Seconda Univ Napoli, Dipartimento Sci Ambientali, I-81100 Caserta, Italy (literal)
- Titolo
- C-terminal truncation of Vascular Endothelial Growth Factor mimetic helical peptide preserves structural and receptor binding properties (literal)
- Abstract
- Vascular Endothelial Growth Factor mimetic peptides have interesting applications in therapeutic angiogenesis. Recently, we described the proangiogenic properties of a 15 mer peptide designed on the N-terminal helix 17-25 of VEGF. The peptide was stabilized introducing well known peptide chemical tools among which N- and C-terminal capping sequence. Here, we show that the C-terminal sequence does not affect the structural and biological properties of the full-length peptide. In fact, a C-terminal truncated analog peptide resulted in a well folded and stable helix retaining the ability to bind to VEGF receptors. This study will allow to develop smaller peptidomimetic analogs able to modulate the VEGF-dependent angiogenesis (literal)
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