Combination of theoretical and experimental approaches for the design and study of fibril-forming peptides
| Autor: | Tamamis, Phanourios, Kasotakis, E., Archontis, Georgios Z., Mitraki, A. |
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| Přispěvatelé: | Archontis, Georgios Z. [0000-0002-7750-8641], Tamamis, Phanourios [0000-0002-3342-2651] |
| Rok vydání: | 2014 |
| Předmět: |
Peptide Biosynthesis
X ray diffraction beta sheet octapeptide transition temperature Molecular dynamics low temperature chemistry Implicit solvent Article Protein Structure Secondary Adenoviridae high temperature fibril forming peptide transmission electron microscopy peptide synthesis Adenovirus nanoribbon protein tertiary structure nanofiber Amyloid fibrils Beta-structure algorithm conformational transition nanofibril adenovirus fiber amyloid Self-assembly peptide uranyl acetate amino acid sequence unclassified drug Nanostructures Protein Structure Tertiary Replica-exchange priority journal physiology nanotube amino terminal sequence nanomaterial protein secondary structure Peptides dodecapeptide |
| Zdroj: | Methods in Molecular Biology Methods Mol. Biol. |
| Popis: | Self-assembling peptides that can form supramolecular structures such as fibrils, ribbons, and nanotubes are of particular interest to modern bionanotechnology and materials science. Their ability to form biocompatible nanostructures under mild conditions through non-covalent interactions offers a big biofabrication advantage. Structural motifs extracted from natural proteins are an important source of inspiration for the rational design of such peptides. Examples include designer self-assembling peptides that correspond to natural coiled-coil motifs, amyloid-forming proteins, and natural fibrous proteins. In this chapter, we focus on the exploitation of structural information from beta-structured natural fibers. We review a case study of short peptides that correspond to sequences from the adenovirus fiber shaft. We describe both theoretical methods for the study of their self-assembly potential and basic experimental protocols for the assessment of fibril-forming assembly. © Springer Science+Business Media New York 2014. 1216 53 70 Cited By :4 |
| Databáze: | OpenAIRE |
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