منابع مشابه
Amyloid Fibrils from Hemoglobin
Amyloid fibrils are a class of insoluble protein nanofibers that are formed via the self-assembly of a wide range of peptides and proteins. They are increasingly exploited for a broad range of applications in bionanotechnology, such as biosensing and drug delivery, as nanowires, hydrogels, and thin films. Amyloid fibrils have been prepared from many proteins, but there has been no definitive ch...
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We consider nucleation of amyloid fibrils in the case when the process occurs by the mechanism of direct polymerization of practically fully extended protein segments, i.e., beta-strands, into beta-sheets. Applying the classical nucleation theory, we derive a general expression for the work to form a nanosized amyloid fibril (protofilament) constituted of successively layered beta-sheets. Analy...
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Herein we report a method to functionalize in vitro grown insulin amyloid fibrils with various inorganic materials. The counterion of the positively charged amyloid fibril is exchanged with anions from various salts; subsequent addition of appropriate cations results in functionalization of the amyloid fibril. We demonstrate the formation of apatite and platinum complex structures ordered by th...
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Protein amyloid fibrils can be functionalized by coating the core protofilament with high concentrations of proteins and enzymes. This can be done elegantly by appending a functional domain to an amyloidogenic protein monomer, then assembling the monomers into a fibril. To display an array of biologically functional porphyrins on the surface of protein fibrils, we have fused the sequence of the...
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Treatment of Alzheimer’s disease (AD) is hampered by the fact that the disease progression cannot be tracked in vivo at this time. Understanding the properties of Aβ amyloid fibrils associated with AD is imperative to finding a way to track the progression of the disease. Recently, fluorescent markers, derived from thioflavin T have been developed as markers of AD. This project examines the int...
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ژورنال
عنوان ژورنال: Prion
سال: 2008
ISSN: 1933-6896,1933-690X
DOI: 10.4161/pri.2.3.7488