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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 (engelsk)Inngår i: ChemBioChem (Print), ISSN 1439-4227, E-ISSN 1439-7633, Vol. 13, nr 3, s. 358-363Artikkel i tidsskrift (Fagfellevurdert) 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.

sted, utgiver, år, opplag, sider
Weinheim, Germany: Wiley-VCH Verlagsgesellschaft, 2012. Vol. 13, nr 3, s. 358-363
Emneord [en]
amyloid beta-peptides; cell binding; cytotoxicity; luminescent conjugated polythiophene (LCP); protein folding
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Identifikatorer
URN: urn:nbn:se:liu:diva-73501DOI: 10.1002/cbic.201100467ISI: 000299834900005OAI: oai:DiVA.org:liu-73501DiVA, id: diva2:473228
Tilgjengelig fra: 2012-01-05 Laget: 2012-01-05 Sist oppdatert: 2018-04-25

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