Zinc Metal Ion Affected the Structural Stability of Amyloid-Like Nanofibrils
| Dublin Core | PKP Metadata Items | Metadata for this Document | |
| 1. | Title | Title of document | Zinc Metal Ion Affected the Structural Stability of Amyloid-Like Nanofibrils |
| 2. | Creator | Author's name, affiliation, country | Zahraa S. Al-Garawi; Physical Biochemistry, Chemistry Departm; Iraq |
| 3. | Subject | Discipline(s) | biology |
| 3. | Subject | Keyword(s) | Functional fibrils, amyloids, structural stability, circular dichroism. |
| 4. | Description | Abstract | Synthetic peptides that self-assemble into well-defined structures with a cross-β arrangement are called amyloid-like fibrils. Amyloids are associated with a list of disorders and neuro-degenerative diseases, such as Alzheimer's and Parkinson`s disease. We previously showed that amyloid-like nanofibrils with a repeating motif “IHIH” were functional fibrils. They were able to bind a metal ion through imidazole moieties and mimic the native carbonic anhydrase enzyme by hydrolysing the CO2 molecule. Thus, these synthetic amyloid fibrils were suggest-ed to be good candidates to moderate and update the modern enzymatic molecules. This study aims to shed a light on the stability of these amyloid nanofibrils over a study period of 25 days, in the presence/absence of a metal ion. The work continued for approximately 7 months in the Biochemistry department, School of Life Sciences at the University of Sussex in the United Kingdom. A set of designed peptides with a repeating motif “IHIH” were ex-plored, based on some structural studies. Short and long peptides with free ends as well as closed ends were investigated. Peptides allowed to self-assemble with and without a metal ion (zinc) were then examined using circular dichroism, fluorimetry and electron microscopy for structural biophysical analysis. Regardless of the metal ion contribution, peptides showed stable secondary structures with a -sheet conformation for the incubation time of 25 days. Their morphologies did not appear to change over time. However, the presence of a zinc ion has an effect on the secondary structure of the mature fibrils. Results indicated that fibrils grown with the zinc ion have a significantly higher propensity to form -sheets secondary structures during incubation time. The presence of a zinc ion also affected the dimensions of the amyloid-like fibrils by the end of the study course, at which point they significantly re-duced. This effect of zinc ion on synthetic amyloid fibrils has not been previously reported. The stabilities of the zinc-nanofibrils point to their potential for use in modifying or updating the enzyme-mimic analytical reactions. The effect of adding zinc on the fibrillation seems to be crucial. Although it apparently improved the -sheet assembly, it affected the width/length of the synthetic amyloids. This effect could be promising toward reducing the generation of amyloid fibrils and ultimately understanding the pathogenesis of Alzheimer disease. |
| 5. | Publisher | Organizing agency, location | Mustansiriyah University |
| 6. | Contributor | Sponsor(s) | |
| 7. | Date | (YYYY-MM-DD) | 2019-03-10 |
| 8. | Type | Status & genre | Peer-reviewed Article |
| 8. | Type | Type | |
| 9. | Format | File format | |
| 10. | Identifier | Uniform Resource Identifier | http://mjs.uomustansiriyah.edu.iq/ojs1/index.php/MJS/article/view/622 |
| 10. | Identifier | Digital Object Identifier (DOI) | http://dx.doi.org/10.23851/mjs.v29i3.622 |
| 11. | Source | Title; vol., no. (year) | Al-Mustansiriyah Journal of Science; Vol 29, No 3 (2018): ICSSSA 2018 Conference Issue |
| 12. | Language | English=en | en |
| 14. | Coverage | Geo-spatial location, chronological period, research sample (gender, age, etc.) | |
| 15. | Rights | Copyright and permissions |
Copyright (c) 2019 Al-Mustansiriyah Journal of Science![]() This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License. |
