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© Research
Publication : Journal of structural biology

The protofilament architecture of a de novo designed coiled coil-based amyloidogenic peptide

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Journal of structural biology - 29 May 2018

de Freitas MS, Rezaei Araghi R, Brandenburg E, Leiterer J, Emmerling F, Folmert K, Gerling-Driessen UIM, Bardiaux B, Böttcher C, Pagel K, Diehl A, Berlepsch HV, Oschkinat H, Koksch B

Link to Pubmed [PMID] – 29857134

J. Struct. Biol. 2018 May;

Amyloid fibrils are polymers formed by proteins under specific conditions and in many cases they are related to pathogenesis, such as Parkinson’s and Alzheimer’s diseases. Their hallmark is the presence of a β-sheet structure. High resolution structural data on these systems as well as information gathered from multiple complementary analytical techniques is needed, from both a fundamental and a pharmaceutical perspective. Here, a previously reported de novo designed, pH-switchable coiled coil-based peptide that undergoes structural transitions resulting in fibril formation under physiological conditions has been exhaustively characterized by transmission electron microscopy (TEM), cryo-TEM, atomic force microscopy (AFM), wide-angle X-ray scattering (WAXS) and solid-state NMR (ssNMR). Overall, a unique 2-dimensional carpet-like assembly composed of large coexisiting ribbon-like, tubular and funnel-like structures with a clearly resolved protofilament substructure is observed. Whereas electron microscopy and scattering data point somewhat more to a hairpin model of β-fibrils, ssNMR data obtained from samples with selectively labelled peptides are in agreement with both, hairpin structures and linear arrangements.

https://www.ncbi.nlm.nih.gov/pubmed/29857134