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Ultrathin silver nanowires produced by amyloid biotemplating
Umeå universitet, Medicinska fakulteten, Institutionen för medicinsk kemi och biofysik.
Umeå universitet, Medicinska fakulteten, Institutionen för medicinsk kemi och biofysik.
2008 (engelsk)Inngår i: Biotechnology progress (Print), ISSN 8756-7938, E-ISSN 1520-6033, Vol. 24, nr 5, s. 1166-1170Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

By using a self-assembled amyloid from lysozyme as biotemplate we produced an ultrathin silver wire of 1 nm diameter and up to 2 μm in length, which is at the limit attainable in nanobiotechnological manufacturing. We showed that 2,2,2-trifluoroethanol produces a dual effect: it reduces ionic silver to colloidal nanoparticles with a regular size, depending on the length of incubation, and induces fibrillar assembly into the amyloid scaffold, forming the hollow channel filled with silver.

sted, utgiver, år, opplag, sider
2008. Vol. 24, nr 5, s. 1166-1170
Emneord [en]
amyloid;biopolymers;biotemplating;nanowires;silver;2, 2, 2-trifluoroethanol
HSV kategori
Identifikatorer
URN: urn:nbn:se:umu:diva-2437DOI: 10.1002/btpr.49OAI: oai:DiVA.org:umu-2437DiVA, id: diva2:140430
Tilgjengelig fra: 2007-06-01 Laget: 2007-06-01 Sist oppdatert: 2018-06-09bibliografisk kontrollert
Inngår i avhandling
1. The amyloid: structure, properties and application
Åpne denne publikasjonen i ny fane eller vindu >>The amyloid: structure, properties and application
2007 (engelsk)Doktoravhandling, med artikler (Annet vitenskapelig)
Abstract [en]

Protein aggregation, leading to the formation and depositions of amyloids, is a cause for a number of diseases such as Alzheimer’s and Creutzfeld-Jacob’s disease, systemic amyloidoses, type II diabetes and others . More than 20 proteins are associated with protein misfolding diseases and even a larger number of proteins can self-assemble into amyloid in vitro. Relating structural and functional properties of amyloid is of particular interest, as this will lead to the identification of the main factors and mechanisms involved in the process of protein misfolding and aggregation; consequently, this will provide a basis for developing new strategies to treat protein misfolding diseases. The aim of the thesis is to investigate structural aspects of amyloid formation and relate that to the functional properties of amyloid. The first paper describes the amyloid formation of equine lysozyme (EL). We have demonstrated that EL enters an amyloid forming pathways under conditions where the molten globule state is populated. We have found that the morphology of the amyloids depend on the calcium-binding to lysozyme, specifically the holo-protein assembles into short, linear protofilaments, while the apo-EL forms ring-shaped structures. The morphology of EL amyloid significantly differs from the amyloid fibrils of human and hen lysozymes. We have suggested that the stable alpha-helical core of EL, which remains structured in the molten globule intermediate, may obstruct the formation of fibrilar interface and therefore leads to assembly of short, curly fibrils and rings.In the second paper, we describe the cytotoxicity of EL amyloids. We have analysed the amyloid intermediates on the pathway towards amyloid fibrils. The sizes of amyloid oligomers were determined by atomic force microscopy (AFM) and the formation of cross-beta sheet was shown by thioflavin T (ThT) binding. The toxicity studies show that the oligomers formed during amyloid growth phase are toxic to a range of cell lines and cultures and the toxicity is size-dependant.The last manuscript describes a novel method for manufacturing of silver nanowires by the biotemplating using amyloid fibrils. The amyloid assembled from an abundant and cheap hen egg white lysozyme was used as a scaffold for casting ultrathin silver nanowires. We have manufactured nanowires with a diameter of 1.0-2.5 nm and up to 2 micrometers in length. Up to date, it is the thinnest silver nanowires produced by using biotemplating and at least one order of magnitude thinner than nanowires manufactured by chemical synthesis.

sted, utgiver, år, opplag, sider
Umeå: Medicinsk kemi och biofysik, 2007. s. 48
Serie
Umeå University medical dissertations, ISSN 0346-6612
Emneord
amyloid, oligomers, AFM, cytotoxicity, biotemplating, lysozyme
HSV kategori
Identifikatorer
urn:nbn:se:umu:diva-1164 (URN)978-91-7264-343-7 (ISBN)
Disputas
2007-09-12, KB3A9, KBC huset, Umeå, 09:00 (engelsk)
Opponent
Veileder
Tilgjengelig fra: 2007-06-01 Laget: 2007-06-01 Sist oppdatert: 2018-03-15bibliografisk kontrollert

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