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Self-assembled bionanostructures: proteins following the lead of DNA nanostructures
Natural polymers are able to self-assemble into versatile nanostructures based on the information encoded into their primary structure. The structural richness of biopolymer-based nanostructures depends on the information content of building blocks and the available biological machinery to assemble...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3938474/ https://www.ncbi.nlm.nih.gov/pubmed/24491139 http://dx.doi.org/10.1186/1477-3155-12-4 |
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author | Gradišar, Helena Jerala, Roman |
author_facet | Gradišar, Helena Jerala, Roman |
author_sort | Gradišar, Helena |
collection | PubMed |
description | Natural polymers are able to self-assemble into versatile nanostructures based on the information encoded into their primary structure. The structural richness of biopolymer-based nanostructures depends on the information content of building blocks and the available biological machinery to assemble and decode polymers with a defined sequence. Natural polypeptides comprise 20 amino acids with very different properties in comparison to only 4 structurally similar nucleotides, building elements of nucleic acids. Nevertheless the ease of synthesizing polynucleotides with selected sequence and the ability to encode the nanostructural assembly based on the two specific nucleotide pairs underlay the development of techniques to self-assemble almost any selected three-dimensional nanostructure from polynucleotides. Despite more complex design rules, peptides were successfully used to assemble symmetric nanostructures, such as fibrils and spheres. While earlier designed protein-based nanostructures used linked natural oligomerizing domains, recent design of new oligomerizing interaction surfaces and introduction of the platform for topologically designed protein fold may enable polypeptide-based design to follow the track of DNA nanostructures. The advantages of protein-based nanostructures, such as the functional versatility and cost effective and sustainable production methods provide strong incentive for further development in this direction. |
format | Online Article Text |
id | pubmed-3938474 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-39384742014-03-01 Self-assembled bionanostructures: proteins following the lead of DNA nanostructures Gradišar, Helena Jerala, Roman J Nanobiotechnology Review Natural polymers are able to self-assemble into versatile nanostructures based on the information encoded into their primary structure. The structural richness of biopolymer-based nanostructures depends on the information content of building blocks and the available biological machinery to assemble and decode polymers with a defined sequence. Natural polypeptides comprise 20 amino acids with very different properties in comparison to only 4 structurally similar nucleotides, building elements of nucleic acids. Nevertheless the ease of synthesizing polynucleotides with selected sequence and the ability to encode the nanostructural assembly based on the two specific nucleotide pairs underlay the development of techniques to self-assemble almost any selected three-dimensional nanostructure from polynucleotides. Despite more complex design rules, peptides were successfully used to assemble symmetric nanostructures, such as fibrils and spheres. While earlier designed protein-based nanostructures used linked natural oligomerizing domains, recent design of new oligomerizing interaction surfaces and introduction of the platform for topologically designed protein fold may enable polypeptide-based design to follow the track of DNA nanostructures. The advantages of protein-based nanostructures, such as the functional versatility and cost effective and sustainable production methods provide strong incentive for further development in this direction. BioMed Central 2014-02-03 /pmc/articles/PMC3938474/ /pubmed/24491139 http://dx.doi.org/10.1186/1477-3155-12-4 Text en Copyright © 2014 Gradišar and Jerala; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Review Gradišar, Helena Jerala, Roman Self-assembled bionanostructures: proteins following the lead of DNA nanostructures |
title | Self-assembled bionanostructures: proteins following the lead of DNA nanostructures |
title_full | Self-assembled bionanostructures: proteins following the lead of DNA nanostructures |
title_fullStr | Self-assembled bionanostructures: proteins following the lead of DNA nanostructures |
title_full_unstemmed | Self-assembled bionanostructures: proteins following the lead of DNA nanostructures |
title_short | Self-assembled bionanostructures: proteins following the lead of DNA nanostructures |
title_sort | self-assembled bionanostructures: proteins following the lead of dna nanostructures |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3938474/ https://www.ncbi.nlm.nih.gov/pubmed/24491139 http://dx.doi.org/10.1186/1477-3155-12-4 |
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