We report on the structural characterization of amyloid-like fibrils, self-assembled from synthetic polypentapeptides poly(ValGlyGlyLeuGly), whose monomeric sequence is a recurring, simple building block of elastin. This polymer adopts a β-sheet structure as revealed by circular dichroism and Fourier transform infrared spectroscopy. Furthermore, Thioflavin-T and Congo red birefringence assays confirm the presence of amyloid-like structures. To analyze the supramolecular assembly and elastic properties of the fibrils, we employed atomic force microsocopy and spectroscopy, measuring also the elasticity of mature elastin for a comparative analysis. In the case of fibrils we estimated a Young’s modulus ranging from 3.5 to 7 MPa, whereas for elastin it is around 1 MPa. The possibility to section individual fibrils with nanometric control by the AFM tip, realizing biomolecular gaps in the 100 nm range, is also demonstrated. These results are expected to open interesting perspectives for the fabrication of protein-inspired nanostructures with specific physical and chemical properties for applications in biotechnology and tissue engineering.

Amyloid-like fibrils in elastin-related polypeptides: Structural characterization and elastic properties

MARUCCIO, Giuseppe;CINGOLANI, Roberto;RINALDI, Rosaria
2008-01-01

Abstract

We report on the structural characterization of amyloid-like fibrils, self-assembled from synthetic polypentapeptides poly(ValGlyGlyLeuGly), whose monomeric sequence is a recurring, simple building block of elastin. This polymer adopts a β-sheet structure as revealed by circular dichroism and Fourier transform infrared spectroscopy. Furthermore, Thioflavin-T and Congo red birefringence assays confirm the presence of amyloid-like structures. To analyze the supramolecular assembly and elastic properties of the fibrils, we employed atomic force microsocopy and spectroscopy, measuring also the elasticity of mature elastin for a comparative analysis. In the case of fibrils we estimated a Young’s modulus ranging from 3.5 to 7 MPa, whereas for elastin it is around 1 MPa. The possibility to section individual fibrils with nanometric control by the AFM tip, realizing biomolecular gaps in the 100 nm range, is also demonstrated. These results are expected to open interesting perspectives for the fabrication of protein-inspired nanostructures with specific physical and chemical properties for applications in biotechnology and tissue engineering.
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: https://hdl.handle.net/11587/329366
 Attenzione

Attenzione! I dati visualizzati non sono stati sottoposti a validazione da parte dell'ateneo

Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 61
  • ???jsp.display-item.citation.isi??? 55
social impact