MARIOS DIMOPOULOS

MARIOS DIMOPOULOS
Marios Dimopoulos Clinical Nutritionist, Author, Fellow of the American Council of the Applied Clinical Nutrition

Τρίτη, 23 Σεπτεμβρίου 2014

Structural properties of EGCG-induced, nontoxic Alzheimer’s disease Aβ oligomers

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Structural properties of EGCG-induced, nontoxic Alzheimer’s disease Aβ oligomers
According to the study by the Deutsches Forschungszentrum für Gesundheit und Umwelt, EGCG interferes with the aromatic hydrophobic core of Aβ. The C-terminal part of the Aβ peptide (residues 22-39) adopts a β-sheet conformation, whereas the N-terminus (residues 1-20) is unstructured. The characteristic salt bridge involving residues D23 and K28 is present in the structure of these oligomeric Aβ aggregates as well. The structural analysis of small-molecule-induced amyloid aggregates will open new perspectives for Alzheimer’s disease drug(24).
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Sources
24. http://www.ncbi.nlm.nih.gov/pubmed/22300765  

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