Studies of luminescent conjugated polythiophene derivatives: enhanced spectral discrimination of protein conformational states

Bioconjug Chem. 2007 Nov-Dec;18(6):1860-8. doi: 10.1021/bc700180g. Epub 2007 Oct 17.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cattle
  • Insulin / chemistry*
  • Polymers / chemical synthesis
  • Polymers / chemistry*
  • Protein Conformation
  • Spectrometry, Fluorescence
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Thiophenes / chemical synthesis
  • Thiophenes / chemistry*
  • Titrimetry
  • Ultracentrifugation

Substances

  • Insulin
  • Polymers
  • Thiophenes
  • polythiophene