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A Fluorescent Pentameric Thiophene Derivative Detects in Vitro-Formed Prefibrillar Protein Aggregates
Linköpings universitet, Institutionen för fysik, kemi och biologi, Biokemi. Linköpings universitet, Tekniska högskolan.ORCID-id: 0000-0001-5827-3587
Linköpings universitet, Institutionen för fysik, kemi och biologi, Organisk Kemi. Linköpings universitet, Tekniska fakulteten.
Linköpings universitet, Institutionen för fysik, kemi och biologi, Biokemi. Linköpings universitet, Tekniska högskolan.ORCID-id: 0000-0002-4303-4783
Linköpings universitet, Institutionen för fysik, kemi och biologi, Organisk Kemi. Linköpings universitet, Tekniska högskolan.
Vise andre og tillknytning
2010 (engelsk)Inngår i: BIOCHEMISTRY, ISSN 0006-2960, Vol. 49, nr 32, s. 6838-6845Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Protein aggregation is associated with a wide range of diseases, and molecular probes that are able to detect a diversity of misfolded protein assemblies are of great importance. The identification of prefibrillar states preceding the formation of well-defined amyloid fibrils is of particular interest both because of their likely role in the mechanism of fibril formation and because of the growing awareness that these species are likely to play a critical role in the pathogenesis of protein deposition diseases. Herein, we explore the use of an anionic oligothiophene derivative, p-FTAA, for detection of prefibrillar protein aggregates during in vitro fibrillation of three different amyloidogenic proteins (insulin, lysozyme, and prion protein). p-FTAA generally detected prefibrillar protein aggregates that could not be detected by thioflavine T fluorescence and in addition showed high fluorescence when bound to mature fibrils. Second, the kinetics of protein aggregation or the formation of amyloid fibrils of insulin was not extensively influenced by the presence of various concentrations of p-FTAA. These results establish the use of p-FTAA as an additional tool for studying the process of protein aggregation.

sted, utgiver, år, opplag, sider
ACS American Chemical Society , 2010. Vol. 49, nr 32, s. 6838-6845
HSV kategori
Identifikatorer
URN: urn:nbn:se:liu:diva-58657DOI: 10.1021/bi100922rISI: 000280668000003OAI: oai:DiVA.org:liu-58657DiVA, id: diva2:344876
Tilgjengelig fra: 2010-08-22 Laget: 2010-08-20 Sist oppdatert: 2019-11-08
Inngår i avhandling
1. Anionic oligothiophenes: Optical tools for multimodal fluorescent assignment of protein aggregates
Åpne denne publikasjonen i ny fane eller vindu >>Anionic oligothiophenes: Optical tools for multimodal fluorescent assignment of protein aggregates
2014 (engelsk)Doktoravhandling, med artikler (Annet vitenskapelig)
Abstract [en]

Luminescent conjugated oligothiophenes (LCOs) represent a useful and interesting class of materials well known for their abilities as transducers for colorimetric and fluorometric reporting. Specifically, they have the ability to produce a conformation-dependent spectral signature reflective of changes in their local environment.  This physical property makes conjugated polymers an indispensible tool in the toolbox of fluorescent reporters used for distinguishing protein aggregates. Because fluorescence measurements provide a number of parameters for observing changes within a system (e.g., changes in intensity, wavelength, energy transfer, and emission lifetime), the coupling of such measurements with the unique fluorescence reporting capabilities of LCOs has been successful in a number of biological systems. The Nilsson group has demonstrated the use of both polydisperse and monodisperse conjugated polythiophenes for the purpose of amyloid protein aggregate detection both in vitro and ex vivo. My doctoral studies have included synthesis and the photophysical evaluation of pentameric substituted oligothiophenes for utilization as molecular probes for investigating the structure and conformation of amyloid protein aggregates. Through the synthesis of a library of pentameric probes with variations in side-chain substituents, we have studied the effects of pH, solvent, and viscosity on probe behavior and spectral shifts to elucidate the role of chemical structure on probe performance. Through a clearer understanding of the nature of LCOs and their individual chromic responses, we hope to provide researchers and clinicians additional tools for investigating and “bringing to light” the multifaceted nature of amyloids.

sted, utgiver, år, opplag, sider
Linköping: Linköping University Electronic Press, 2014. s. 41
Serie
Linköping Studies in Science and Technology. Dissertations, ISSN 0345-7524 ; 1630
HSV kategori
Identifikatorer
urn:nbn:se:liu:diva-111657 (URN)978-91-7519-205-5 (ISBN)
Disputas
2014-11-14, Visionen B-huset, Campus Valla, Linköpings universitet, Linköping, 09:15 (engelsk)
Opponent
Veileder
Tilgjengelig fra: 2014-10-28 Laget: 2014-10-28 Sist oppdatert: 2014-10-28bibliografisk kontrollert

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Hammarström, PerSimon, RozalynNyström, SofieKonradsson, PeterÅslund, AndreasNilsson, Peter

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