Neuroserpin and transthyretin are extracellular chaperones that preferentially inhibit amyloid formation

Author:

West Jennifer12ORCID,Satapathy Sandeep12ORCID,Whiten Daniel R.3ORCID,Kelly Megan4ORCID,Geraghty Nicholas J.12ORCID,Proctor Emma-Jayne2ORCID,Sormanni Pietro5ORCID,Vendruscolo Michele5ORCID,Buxbaum Joel N.67ORCID,Ranson Marie2ORCID,Wilson Mark R.12ORCID

Affiliation:

1. Molecular Horizons and School of Chemistry and Molecular Bioscience, University of Wollongong, Northfields Avenue, Wollongong, NSW 2522, Australia.

2. Illawarra Health and Medical Research Institute, Northfields Avenue, Wollongong, NSW 2522, Australia.

3. Kolling Institute of Medical Research, University of Sydney, NSW 2065, Australia.

4. School of Medicine, University of Wollongong, Northfields Avenue, Wollongong, NSW 2522, Australia.

5. Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.

6. The Scripps Research Institute, La Jolla, CA, USA.

7. Protego Biopharma, La Jolla, CA, USA.

Abstract

Neuroserpin preferentially inhibits amyloid formation; a 14-mer region in neuroserpin is implicated in binding to amyloid.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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