ISSN:
1573-3904
Keywords:
Aβ(1-40)
;
acetylHmb
;
circular dichroism
;
electron microscopy
;
fibril formation
;
secondary structure
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract 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).
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1008931309727
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