The Polyphenol EGCG Inhibits Amyloid Formation Less Efficiently at Phospholipid Interfaces than in Bulk Solution-Reference-Cited by-同舟云学术

The Polyphenol EGCG Inhibits Amyloid Formation Less Efficiently at Phospholipid Interfaces than in Bulk Solution

Published:2012-08-27 Issue:36 Volume:134 Page:14781-14788
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Engel Maarten F. M.¹,vandenAkker Corianne C.¹,Schleeger Michael¹²,Velikov Krassimir P.³⁴,Koenderink Gijsje H.¹,Bonn Mischa¹²

Affiliation:

1. FOM Institute AMOLF, Science Park 104, 1098 XG, Amsterdam, The Netherlands

2. Department of Molecular Spectroscopy, Max Planck Institute for Polymer Research, Ackermannweg 10, 55128 Mainz, Germany

3. Unilever R&D Vlaardingen, Olivier van Noortlaan 120, 3133 AT Vlaardingen, The Netherlands

4. Soft Condensed Matter, Debye Institute for Nanomaterials Science, Department of Physics and Astronomy, Utrecht University, Princetonplein 5, 3584 CC, Utrecht, The Netherlands

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja3031664

Reference62 articles.

1. Protein Misfolding, Functional Amyloid, and Human Disease

2. Islet Amyloid and Type 2 Diabetes Mellitus

3. Membrane permeabilization by Islet Amyloid Polypeptide

4. Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis

5. Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?

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