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Cell Interaction Study of Amyloid by Using Luminescent Conjugated Polythiophene: Implication that Amyloid Cytotoxicity Is Correlated withProlonged Cellular Binding
Bioengineering Laboratory, RIKEN Institute, Wako, Saitama, Japan.
Bioengineering Laboratory, RIKEN Institute, Wako, Saitama, Japan.
(Bioengineering Laboratory, RIKEN Institute, Wako, Saitama, Japan)
Bioengineering Laboratory, RIKEN Institute, Wako, Saitama, Japan.
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2012 (English)In: ChemBioChem (Print), ISSN 1439-4227, E-ISSN 1439-7633, Vol. 13, no 3, 358-363 p.Article in journal (Refereed) Published
Abstract [en]

Needles and noodles: Studying amyloid toxicity is important for understanding protein misfolding diseases. Using a luminescent conjugated polythiophene, we found that cell binding of nontoxic filamentous amyloids of insulin and β2-microglobulin was less efficient than that of toxic fibrillar amyloids; this suggests a correlation between amyloid toxicity and cell binding.

Place, publisher, year, edition, pages
Weinheim, Germany: Wiley-VCH Verlagsgesellschaft, 2012. Vol. 13, no 3, 358-363 p.
Keyword [en]
amyloid beta-peptides; cell binding; cytotoxicity; luminescent conjugated polythiophene (LCP); protein folding
National Category
Cell and Molecular Biology
Identifiers
URN: urn:nbn:se:liu:diva-73501DOI: 10.1002/cbic.201100467ISI: 000299834900005OAI: oai:DiVA.org:liu-73501DiVA: diva2:473228
Available from: 2012-01-05 Created: 2012-01-05 Last updated: 2017-12-08

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Nilsson, PeterHammarström, Per

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