Effect of ferric citrate on amyloid-beta peptides behavior
Autor: | Cristina D'Arrigo, Denise Galante, Angelo Perico, E. Cavallo |
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Rok vydání: | 2017 |
Předmět: |
0301 basic medicine
Circular dichroism Time Factors Amyloid beta Iron Biophysics Ethylenediaminetetraacetic acid Iron Chelating Agents Biochemistry Ferric Compounds Phase Transition Biomaterials 03 medical and health sciences chemistry.chemical_compound Aspartic acid Chelation Benzothiazoles Tyrosine Amyloid beta-Peptides biology Chemistry Circular Dichroism Organic Chemistry General Medicine Glutamic acid Thiazoles 030104 developmental biology Spectrometry Fluorescence biology.protein |
Zdroj: | Biopolymers. 109(6) |
ISSN: | 1097-0282 |
Popis: | Amyloid beta (Aβ) aggregation and oxidative stress are two of the central events in Alzheimer's Disease (AD). Both these phenomena can be caused by the interaction of Aβ with metal ions. In the last years the interaction between ZnII , CuII , and Aβ was much studied, but between iron and Aβ it is still little known. In this work we determine how three Aβ peptides, present in AD, interact with FeIII -citrate. The three Aβ peptides are: full length Aβ1-42, an isoform truncated at Glutamic acid in position three, Aβ3-42, and its pyroglutamated form AβpE3-42. Conformation and morphology of the three peptides, aggregated with and without FeIII -citrate were studied. Besides, we have determined the strength of the interactions Aβ/FeIII -citrate studying the effect of ethylenediaminetetraacetic acid as chelator. Results reported here demonstrate that FeIII -citrate promotes the aggregation in all the three peptides. Moreover, Aspartic acid 1, Glutamic acid 3, and Tyrosine 10 have an important role in the coordination with iron, generating a more stable complex for Aβ1-42 compared to that for the truncated peptides. |
Databáze: | OpenAIRE |
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