Modulating the Folding Landscape of Superoxide Dismutase 1 with Targeted Molecular Binders.

Autor: Bunck DN; Division of Chemistry and Chemical Engineering, California Institute of Technology, 1200 East California Boulevard, MC, 172-27, USA., Atsavapranee B; Division of Chemistry and Chemical Engineering, California Institute of Technology, 1200 East California Boulevard, MC, 172-27, USA., Museth AK; Division of Chemistry and Chemical Engineering, California Institute of Technology, 1200 East California Boulevard, MC, 172-27, USA., VanderVelde D; Division of Chemistry and Chemical Engineering, California Institute of Technology, 1200 East California Boulevard, MC, 172-27, USA., Heath JR; Division of Chemistry and Chemical Engineering, California Institute of Technology, 1200 East California Boulevard, MC, 172-27, USA.
Jazyk: angličtina
Zdroj: Angewandte Chemie (International ed. in English) [Angew Chem Int Ed Engl] 2018 May 22; Vol. 57 (21), pp. 6212-6215. Date of Electronic Publication: 2018 Apr 25.
DOI: 10.1002/anie.201802269
Abstrakt: Amyotrophic lateral sclerosis, or Lou Gehrig's disease, is characterized by motor neuron death, with average survival times of two to five years. One cause of this disease is the misfolding of superoxide dismutase 1 (SOD1), a phenomenon influenced by point mutations spanning the protein. Herein, we used an epitope-specific high-throughput screen to identify a peptide ligand that stabilizes the SOD1 native conformation and accelerates its folding by a factor of 2.5. This strategy may be useful for fundamental studies of protein energy landscapes as well as designing new classes of therapeutics.
(© 2018 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.)
Databáze: MEDLINE
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