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Nanomaterials: amyloids reflect their brighter side
Amyloid fibrils belong to the group of ordered nanostructures that are self-assembled from a wide range of polypeptides/proteins. Amyloids are highly rigid structures possessing a high mechanical strength. Although amyloids have been implicated in the pathogenesis of several human diseases, growing...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
CoAction Publishing
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3215191/ https://www.ncbi.nlm.nih.gov/pubmed/22110868 http://dx.doi.org/ 10.3402/nano.v2i0.6032 |
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author | Mankar, Shruti Anoop, A. Sen, Shamik Maji, Samir K. |
author_facet | Mankar, Shruti Anoop, A. Sen, Shamik Maji, Samir K. |
author_sort | Mankar, Shruti |
collection | PubMed |
description | Amyloid fibrils belong to the group of ordered nanostructures that are self-assembled from a wide range of polypeptides/proteins. Amyloids are highly rigid structures possessing a high mechanical strength. Although amyloids have been implicated in the pathogenesis of several human diseases, growing evidence indicates that amyloids may also perform native functions in host organisms. Discovery of such amyloids, referred to as functional amyloids, highlight their possible use in designing novel nanostructure materials. This review summarizes recent advances in the application of amyloids for the development of nanomaterials and prospective applications of such materials in nanotechnology and biomedicine. |
format | Online Article Text |
id | pubmed-3215191 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | CoAction Publishing |
record_format | MEDLINE/PubMed |
spelling | pubmed-32151912011-11-22 Nanomaterials: amyloids reflect their brighter side Mankar, Shruti Anoop, A. Sen, Shamik Maji, Samir K. Nano Rev Review Article Amyloid fibrils belong to the group of ordered nanostructures that are self-assembled from a wide range of polypeptides/proteins. Amyloids are highly rigid structures possessing a high mechanical strength. Although amyloids have been implicated in the pathogenesis of several human diseases, growing evidence indicates that amyloids may also perform native functions in host organisms. Discovery of such amyloids, referred to as functional amyloids, highlight their possible use in designing novel nanostructure materials. This review summarizes recent advances in the application of amyloids for the development of nanomaterials and prospective applications of such materials in nanotechnology and biomedicine. CoAction Publishing 2011-05-31 /pmc/articles/PMC3215191/ /pubmed/22110868 http://dx.doi.org/ 10.3402/nano.v2i0.6032 Text en © 2011 Shruti Mankar et al. http://creativecommons.org/licenses/by-nc/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution-Noncommercial 3.0 Unported License, permitting all non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Article Mankar, Shruti Anoop, A. Sen, Shamik Maji, Samir K. Nanomaterials: amyloids reflect their brighter side |
title | Nanomaterials: amyloids reflect their brighter side |
title_full | Nanomaterials: amyloids reflect their brighter side |
title_fullStr | Nanomaterials: amyloids reflect their brighter side |
title_full_unstemmed | Nanomaterials: amyloids reflect their brighter side |
title_short | Nanomaterials: amyloids reflect their brighter side |
title_sort | nanomaterials: amyloids reflect their brighter side |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3215191/ https://www.ncbi.nlm.nih.gov/pubmed/22110868 http://dx.doi.org/ 10.3402/nano.v2i0.6032 |
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