Studies of luminescent conjugated polythiophene derivatives-Enhanced spectral discrimination of protein conformational states
2007 (English)In: Bioconjugate chemistry, ISSN 1043-1802, E-ISSN 1520-4812, Vol. 18, no 6, 1860-1868 p.Article in journal (Refereed) Published
Improved probes for amyloid fibril formation are advantageous for the early detection and better understanding of this disease-associated process. Here, we report a comparative study of eight luminescent conjugated polythiophene derivates (LCPs) and their discrimination of a protein (insulin) in the native or amyloid-like fibrillar state. For two of the LCPs, the synthesis is reported. Compared to their monomer-based analogues, trimer-based LCPs showed significantly better optical signal specificity for amyloid-like fibrils, seen from increased quantum yield and spectral shift. The trimer-based LCPs alone were highly quenched and showed little interaction with native insulin, as seen from analytical ultracentrifugation and insignificant spectral differences from the trimer-based LCP in buffered and native protein solution. Hence, the trimer-based LCPs showed enhanced discrimination between the amyloid-like fibrillar state and the corresponding native protein.
Place, publisher, year, edition, pages
2007. Vol. 18, no 6, 1860-1868 p.
IdentifiersURN: urn:nbn:se:liu:diva-14600DOI: 10.1021/bc700180gOAI: oai:DiVA.org:liu-14600DiVA: diva2:23993