The Route from the Folded to the Amyloid State: Exploring the Potential Energy Surface of a Drug-Like Miniprotein

Nóra Taricska; Dániel Horváth; Dóra K Menyhárd; Hanna Ákontz-Kiss; Masahiro Noji; Masatomo So; Yuji Goto; Toshimichi Fujiwara; András Perczel

doi:10.1002/chem.201905181

The Route from the Folded to the Amyloid State: Exploring the Potential Energy Surface of a Drug-Like Miniprotein

Chemistry. 2020 Feb 11;26(9):1893. doi: 10.1002/chem.201905181. Epub 2020 Jan 21.

Authors

Nóra Taricska¹, Dániel Horváth¹, Dóra K Menyhárd¹, Hanna Ákontz-Kiss¹, Masahiro Noji², Masatomo So², Yuji Goto², Toshimichi Fujiwara², András Perczel¹

Affiliations

¹ Laboratory of Structural Chemistry and Biology &, MTA-ELTE Protein Modeling Research Group, Eötvös Loránd University, Pázmány Péter sétány 1A, 1117, Budapest, Hungary.
² Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka, 565-0871, Japan.

PMID: 31961031
DOI: 10.1002/chem.201905181

Abstract

Invited for the cover of this issue is the group of András Perczel at Eötvös Loránd University, Budapest, Hungary and colleagues from Osaka University, Japan. The image depicts the amyloid buildup of an Exenatide derivate miniprotein (E5) monitored on a simplified hyperspace. Read the full text of the article at 10.1002/chem.201903826.

MeSH terms

Amyloid / chemistry
Amyloid / metabolism*
Models, Biological
Nuclear Magnetic Resonance, Biomolecular
Peptides / chemistry
Peptides / metabolism
Protein Structure, Secondary
Thermodynamics

Substances

Amyloid
Peptides