Secondary structural modifications of Aβ(1–40) induced by multiple 2-acetoxy-4-methoxybenzyl (acetylHmb) protection
| Autor: | John D. Wade, Mary Macris, Weilan He, Andrew B. Clippingdale, Colin J. Barrow |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
chemistry.chemical_classification
Circular dichroism Chemistry Pharmacology toxicology Bioengineering Peptide Biochemistry Analytical Chemistry law.invention Crystallography chemistry.chemical_compound Fibril formation law Amide Drug Discovery Molecular Medicine Electron microscope Protein secondary structure |
| Zdroj: | Letters in Peptide Science. 6:289-293 |
| ISSN: | 1573-3904 0929-5666 |
| DOI: | 10.1007/bf02443424 |
| Popis: | Modifications to secondary structure and fibril formation caused by multiple acetylHmb backbone amide protection of Alzheimer's disease Aβ(1-40) were investigated using circular dichroism spectroscopy and electron microscopy. Penta(acetylHmb)Aβ(1-40) was observed to have a reduced ability to form α-helix and β-sheet structures under the same solution conditions as the native peptide, with α-helical propensity being reduced more significantly than β-sheet propensity. Further, acetylHmb backbone protection was found to alter Aβ(1-40) interaction with SDS-micelles by preventing α-helix formation. Aβ fibril formation, a characteristic property of this peptide, was also not observed for penta(acetylHmb)Aβ(1-40). |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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