Oriented epitaxial growth of amyloid fibrils of the N27C mutant beta 25-35 peptide
| Autor: | Ünige Murvai, Miklós S.Z. Kellermayer, Katalin Soós, Árpád Karsai, Botond Penke |
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| Rok vydání: | 2007 |
| Předmět: |
Amyloid
Time Factors Biophysics Beta sheet Membrane biology Peptide Fibril Microscopy Atomic Force Residue (chemistry) Cations Extracellular Nanotechnology Amino Acid Sequence Cysteine chemistry.chemical_classification Amyloid beta-Peptides General Medicine Peptide Fragments Biomechanical Phenomena Crystallography chemistry Mutation Aluminum Silicates Protein Binding |
| Zdroj: | European biophysics journal : EBJ. 37(7) |
| ISSN: | 0175-7571 |
| Popis: | Amyloid fibrils are present in the extracellular space of various tissues in neurodegenerative and protein misfolding diseases. Amyloid fibrils may be used in nanotechnology applications, because of their self-assembly properties and stability, if their growth and orientation can be controlled. Recently, we have shown that amyloid beta 25-35 (A beta 25-35) forms a highly oriented, K(+)-dependent network on mica. Here, we analyzed the properties of A beta 25-35_N27C, the cysteine residue of which may be used for subsequent chemical modifications. We find that A beta 25-35_N27C forms epitaxially growing fibrils on mica, which evolve into a trigonally oriented branched network. The binding is apparently more sensitive to cation concentration than that of the wild-type peptide. By nanomanipulating A beta 25-35_N27C fibrils with a gold-coated AFM tip, we show that the sulfhydryl of Cys27 is reactive and accessible from the solution. The oriented network of A beta 25-35_N27C fibrils can therefore be specifically labeled and may be used for constructing nanobiotechnological devices. |
| Databáze: | OpenAIRE |
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