Investigating the Amyloidogenic Nanostructured Sequences of Elastin: Sequence Encoded by Exon 28 of Human Tropoelastin Gene
| Autor: | Antonietta Pepe, Brigida Bochicchio, R Flamia, Marina Lorusso, Antonio Mario Tamburro |
|---|---|
| Rok vydání: | 2007 |
| Předmět: |
Amyloid
Circular dichroism Magnetic Resonance Spectroscopy Time Factors Polymers and Plastics Bioengineering macromolecular substances Microscopy Atomic Force Fibril Biomaterials Tropoelastin Spectroscopy Fourier Transform Infrared Materials Chemistry Humans Fourier transform infrared spectroscopy Protein secondary structure biology Chemistry Circular Dichroism Congo Red Exons Elastin Crystallography Helix Microscopy Electron Scanning biology.protein Ultrastructure |
| Zdroj: | Biomacromolecules. 8:3478-3486 |
| ISSN: | 1526-4602 1525-7797 |
| DOI: | 10.1021/bm700636a |
| Popis: | In this paper we demonstrate that the sequence encoded by exon 28 (EX28) of human tropoelastin gene is able to give amyloid-like fibrils. CD (circular dichroism) in solution and solid-state FTIR (Fourier transform infrared spectroscopy) spectroscopies have shown the presence of beta-sheet conformation. At the supramolecular level the fibers formed by EX28 peptide were investigated by AFM (atomic force microscopy) and ESEM (environmental scanning electron microscopy). A very big left-handed helix, 100 mum long, is visible together with aggregates of different sizes, some of them being constituted by helically interwoven fibers. Furthermore, an additional AFM image of EX28 is shown where the ultrastructure found is somewhat reminiscent of a more or less retiform film. These findings should be useful for designing proper elastin-inspired biomaterials. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|