Infrared nanospectroscopy reveals the molecular interaction fingerprint of an aggregation inhibitor with single Aβ42 oligomers

Francesco Simone Ruggeri; Johnny Habchi; Sean Chia; Robert I. Horne; Michele Vendruscolo; Tuomas P. J. Knowles

doi:10.1038/s41467-020-20782-0

Nature Communications (Jan 2021)

Infrared nanospectroscopy reveals the molecular interaction fingerprint of an aggregation inhibitor with single Aβ42 oligomers

Francesco Simone Ruggeri,
Johnny Habchi,
Sean Chia,
Robert I. Horne,
Michele Vendruscolo,
Tuomas P. J. Knowles

Affiliations

Francesco Simone Ruggeri: Department of Chemistry, Center for Misfolding Diseases, University of Cambridge
Johnny Habchi: Department of Chemistry, Center for Misfolding Diseases, University of Cambridge
Sean Chia: Department of Chemistry, Center for Misfolding Diseases, University of Cambridge
Robert I. Horne: Department of Chemistry, Center for Misfolding Diseases, University of Cambridge
Michele Vendruscolo: Department of Chemistry, Center for Misfolding Diseases, University of Cambridge
Tuomas P. J. Knowles: Department of Chemistry, Center for Misfolding Diseases, University of Cambridge

DOI: https://doi.org/10.1038/s41467-020-20782-0
Journal volume & issue: Vol. 12, no. 1
pp. 1 – 9

Abstract

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Our understanding of the molecular mechanisms underlying pathological protein aggregation remains incomplete. Here, single molecule infrared nanospectroscopy (AFM-IR) offers insight into the structure of Aβ42 oligomeric and fibrillar species and their interaction with an aggregation inhibitor, paving the way for single molecule drug discovery studies.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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