Spectroscopic Characterization of Nonnative Conformational States of Cytochromec

Silke Oellerich; Hainer Wackerbarth; Peter Hildebrandt

doi:10.1021/jp013841g

Spectroscopic Characterization of Nonnative Conformational States of Cytochromec

The Journal of Physical Chemistry B ◽

10.1021/jp013841g ◽

2002 ◽

Vol 106 (25) ◽

pp. 6566-6580 ◽

Cited By ~ 159

Author(s):

Silke Oellerich ◽

Hainer Wackerbarth ◽

Peter Hildebrandt

Keyword(s):

Spectroscopic Characterization ◽

Conformational States

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Spectroscopic characterization of the conformational states of the bis(trifluoromethanesulfonyl)imide anion (TFSI−)

Journal of Raman Spectroscopy ◽

10.1002/jrs.1347 ◽

2005 ◽

Vol 36 (8) ◽

pp. 762-770 ◽

Cited By ~ 226

Author(s):

M. Herstedt ◽

M. Smirnov ◽

P. Johansson ◽

M. Chami ◽

J. Grondin ◽

...

Keyword(s):

Spectroscopic Characterization ◽

Conformational States

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Spectroscopic Characterization of Intermolecular Interaction of AmyloidβPromoted on GM1 Micelles

International Journal of Alzheimer s Disease ◽

10.4061/2011/925073 ◽

2011 ◽

Vol 2011 ◽

pp. 1-8 ◽

Cited By ~ 14

Author(s):

Maho Yagi-Utsumi ◽

Koichi Matsuo ◽

Katsuhiko Yanagisawa ◽

Kunihiko Gekko ◽

Koichi Kato

Keyword(s):

Intermolecular Interaction ◽

Conformational Transition ◽

Spectroscopic Characterization ◽

Thioflavin T ◽

Helical Structures ◽

Conformational States ◽

Hydrophobic Anchor

Clusters of GM1 gangliosides act as platforms for conformational transition of monomeric, unstructured amyloidβ(Aβ) to its toxicβ-structured aggregates. We have previously shown that Aβ(1–40) accommodated on the hydrophobic/hydrophilic interface of lyso-GM1 or GM1 micelles assumesα-helical structures under ganglioside-excess conditions. For better understanding of the mechanisms underlying theα-to-βconformational transition of Aβon GM1 clusters, we performed spectroscopic characterization of Aβ(1–40) titrated with GM1. It was revealed that the thioflavin T- (ThT-) reactiveβ-structure is more populated in Aβ(1–40) under conditions where the Aβ(1–40) density on GM1 micelles is high. Under this circumstance, the C-terminal hydrophobic anchor Val39-Val40shows two distinct conformational states that are reactive with ThT, while such Aβspecies were not generated by smaller lyso-GM1 micelles. These findings suggest that GM1 clusters promote specific Aβ-Aβinteractions through their C-termini coupled with formation of the ThT-reactiveβ-structure depending on sizes and curvatures of the clusters.

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