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Issue 5, 2016
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Comparison of strategies for non-perturbing labeling of α-synuclein to study amyloidogenesis

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Abstract

Characterization of the amyloidogenic Parkinson's disease protein α-synuclein (αS) has proven difficult due to its structural plasticity. Here, we present a number of complementary methods to site-specifically introduce fluorescent probes to examine αS fibril formation and cellular uptake. By using various combinations of conventional Cys modification, amber codon suppression, transferase mediated N-terminal modification, and native chemical ligation, several variants of singly- and doubly-labeled αS were produced. We validated the nonperturbative nature of the label by a combination of in vitro aggregation kinetics measurements and imaging of the resulting fibrils. The labeled αS can then be used to monitor conformational changes during fibril formation or cellular uptake of αS fibrils in models of disease propagation.

Graphical abstract: Comparison of strategies for non-perturbing labeling of α-synuclein to study amyloidogenesis

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Submitted
12 Nov 2015
Accepted
14 Dec 2015
First published
22 Dec 2015

Org. Biomol. Chem., 2016,14, 1584-1592
Article type
Paper
Author version available

Comparison of strategies for non-perturbing labeling of α-synuclein to study amyloidogenesis

C. M. Haney, R. F. Wissner, J. B. Warner, Y. J. Wang, J. J. Ferrie, D. J. Covell, R. J. Karpowicz, V. M.-Y. Lee and E. James Petersson, Org. Biomol. Chem., 2016, 14, 1584
DOI: 10.1039/C5OB02329G

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