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Zn(2+) Interaction with Amyloid-B: Affinity and Speciation
Conflicting values, obtained by different techniques and often under different experimental conditions have been reported on the affinity of Zn(2+) for amyloid-β, that is recognized as the major interaction responsible for Alzheimer’s disease. Here, we compare the approaches employed so far, i.e., t...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6695645/ https://www.ncbi.nlm.nih.gov/pubmed/31370315 http://dx.doi.org/10.3390/molecules24152796 |
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author | Arena, Giuseppe Rizzarelli, Enrico |
author_facet | Arena, Giuseppe Rizzarelli, Enrico |
author_sort | Arena, Giuseppe |
collection | PubMed |
description | Conflicting values, obtained by different techniques and often under different experimental conditions have been reported on the affinity of Zn(2+) for amyloid-β, that is recognized as the major interaction responsible for Alzheimer’s disease. Here, we compare the approaches employed so far, i.e., the evaluation of K(d) and the determination of the stability constants to quantitatively express the affinity of Zn(2+) for the amyloid-β peptide, evidencing the pros and cons of the two approaches. We also comment on the different techniques and conditions employed that may lead to divergent data. Through the analysis of the species distribution obtained for two selected examples, we show the implications that the speciation, based on stoichiometric constants rather than on K(d), may have on data interpretation. The paper also demonstrates that the problem is further complicated by the occurrence of multiple equilibria over a relatively narrow pH range. |
format | Online Article Text |
id | pubmed-6695645 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-66956452019-09-05 Zn(2+) Interaction with Amyloid-B: Affinity and Speciation Arena, Giuseppe Rizzarelli, Enrico Molecules Review Conflicting values, obtained by different techniques and often under different experimental conditions have been reported on the affinity of Zn(2+) for amyloid-β, that is recognized as the major interaction responsible for Alzheimer’s disease. Here, we compare the approaches employed so far, i.e., the evaluation of K(d) and the determination of the stability constants to quantitatively express the affinity of Zn(2+) for the amyloid-β peptide, evidencing the pros and cons of the two approaches. We also comment on the different techniques and conditions employed that may lead to divergent data. Through the analysis of the species distribution obtained for two selected examples, we show the implications that the speciation, based on stoichiometric constants rather than on K(d), may have on data interpretation. The paper also demonstrates that the problem is further complicated by the occurrence of multiple equilibria over a relatively narrow pH range. MDPI 2019-07-31 /pmc/articles/PMC6695645/ /pubmed/31370315 http://dx.doi.org/10.3390/molecules24152796 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Arena, Giuseppe Rizzarelli, Enrico Zn(2+) Interaction with Amyloid-B: Affinity and Speciation |
title | Zn(2+) Interaction with Amyloid-B: Affinity and Speciation |
title_full | Zn(2+) Interaction with Amyloid-B: Affinity and Speciation |
title_fullStr | Zn(2+) Interaction with Amyloid-B: Affinity and Speciation |
title_full_unstemmed | Zn(2+) Interaction with Amyloid-B: Affinity and Speciation |
title_short | Zn(2+) Interaction with Amyloid-B: Affinity and Speciation |
title_sort | zn(2+) interaction with amyloid-b: affinity and speciation |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6695645/ https://www.ncbi.nlm.nih.gov/pubmed/31370315 http://dx.doi.org/10.3390/molecules24152796 |
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