Quantitative Measurement of the Affinity of Toxic and Nontoxic Misfolded Protein Oligomers for Lipid Bilayers and of its Modulation by Lipid Composition and Trodusquemine-Reference-Cited by-同舟云学术

Quantitative Measurement of the Affinity of Toxic and Nontoxic Misfolded Protein Oligomers for Lipid Bilayers and of its Modulation by Lipid Composition and Trodusquemine

Published:2021-08-12 Issue:17 Volume:12 Page:3189-3202
ISSN:1948-7193
Container-title:ACS Chemical Neuroscience
language:en
Short-container-title:ACS Chem. Neurosci.

Author:

Errico Silvia¹²,Ramshini Hassan¹³,Capitini Claudia⁴⁵,Canale Claudio⁶,Spaziano Martina¹,Barbut Denise⁷,Calamai Martino⁴⁸^ORCID,Zasloff Michael⁷⁹,Oropesa-Nuñez Reinier¹⁰^ORCID,Vendruscolo Michele²^ORCID,Chiti Fabrizio¹^ORCID

Affiliation:

1. Department of Experimental and Clinical Biomedical Sciences, Section of Biochemistry, University of Florence, Florence 50134, Italy

2. Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom

3. Department of Biology, Payame Noor University, Tehran 19395-4697, Islamic Republic of Iran

4. European Laboratory for Non-linear Spectroscopy (LENS), Sesto Fiorentino 50019, Italy

5. Department of Physics and Astronomy, University of Florence, Sesto Fiorentino 50019, Italy

6. Department of Physics, University of Genoa, Genoa 16146, Italy

7. Enterin Inc., 2005 Market Street, Philadelphia, Pennsylvania 19103, United States

8. National Institute of Optics, National Research Council of Italy (CNR), Florence 50125, Italy

9. MedStar-Georgetown Transplant Institute, Georgetown University School of Medicine, Washington D.C. 20007, United States

10. Department of Materials Science and Engineering, Uppsala University, Uppsala SE-751 03, Sweden

Funder

Ministero dellâ??Istruzione, dellâ??UniversitÃ e della Ricerca

Regione Toscana

Horizon 2020 Framework Programme

UniversitÃ degli Studi di Firenze

Publisher

American Chemical Society (ACS)

Subject

Cell Biology,Cognitive Neuroscience,Physiology,Biochemistry,General Medicine

Link

https://pubs.acs.org/doi/pdf/10.1021/acschemneuro.1c00327

Reference59 articles.

1. Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade

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3. Reduction of the amyloidogenicity of a protein by specific binding of ligands to the native conformation

4. Amyloid Fibril Formation and Disaggregation of Fragment 1-29 of Apomyoglobin: Insights into the Effect of pH on Protein Fibrillogenesis

5. Experimental free energy surfaces reveal the mechanisms of maintenance of protein solubility

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