2. Academic Validation
  3. Crocus-derived compounds alter the aggregation pathway of Alzheimer's Disease: associated beta amyloid protein

Crocus-derived compounds alter the aggregation pathway of Alzheimer's Disease: associated beta amyloid protein

  • Sci Rep. 2020 Oct 23;10(1):18150. doi: 10.1038/s41598-020-74770-x.
Nikolaos Stavros Koulakiotis 1,  Pasi Purhonen 2,  Evangelos Gikas 3,  Hans Hebert 2,  Anthony Tsarbopoulos 4 5
Affiliations

Affiliations

  • 1 GAIA Research Center, Bioanalytical Department, The Goulandris Natural History Museum, 14562, Kifissia, Greece.
  • 2 School of Engineering Sciences in Chemistry, Biotechnology and Health, Department of Biomedical Engineering and Health Systems, KTH Royal Institute of Technology, S-141 52, Huddinge, Sweden.
  • 3 Department of Pharmacy, National and Kapodistrian University of Athens, 15771, Athens, Greece.
  • 4 GAIA Research Center, Bioanalytical Department, The Goulandris Natural History Museum, 14562, Kifissia, Greece. [email protected].
  • 5 Department of Pharmacology, National and Kapodistrian University of Athens Medical School, 75 Mikras Asias Street, 11527, Athens, Greece. [email protected].
PMID: 33097779 DOI: 10.1038/s41598-020-74770-x
Abstract

Natural Products have played a dominant role in the discovery of lead compounds for the development of drugs aimed at the treatment of human diseases. This electrospray ionization-ion mobility spectrometry-mass spectrometry (ESI-IMS-MS)-based study demonstrates that dietary antioxidants, isolated components from the stigmas of saffron (Crocus sativus L.) may be effective in inhibiting Aβ fibrillogenesis, a neuropathological hallmark of Alzheimer's Disease (AD). This study reveals a substantial alteration in the monomer/oligomer distribution of Aβ1-40, concomitant with re-direction of fibril formation, induced by the natural product interaction. These alterations on the Aβ1-40 aggregation pathway are most prominent for trans-crocin-4 (TC4). Use of ESI-IMS-MS, electron microscopy alongside Thioflavin-T kinetics, and the interpretation of 3-dimensional Driftscope plots indicate a correlation of these monomer/oligomer distribution changes with alterations to Aβ1-40 amyloid formation. The latter could prove instrumental in the development of novel aggregation inhibitors for the prevention, or treatment of AD.

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