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Engineering building blocks for self-assembling protein nanoparticles

Like natural viruses, manmade protein cages for drug delivery are to be ideally formed by repetitive subunits with self-assembling properties, mimicking viral functions and molecular organization. Naturally formed nanostructures (such as viruses, flagella or simpler protein oligomers) can be enginee...

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Detalles Bibliográficos
Autores principales: Vázquez, Esther, Villaverde, Antonio
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3022712/
https://www.ncbi.nlm.nih.gov/pubmed/21192790
http://dx.doi.org/10.1186/1475-2859-9-101
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author Vázquez, Esther
Villaverde, Antonio
author_facet Vázquez, Esther
Villaverde, Antonio
author_sort Vázquez, Esther
collection PubMed
description Like natural viruses, manmade protein cages for drug delivery are to be ideally formed by repetitive subunits with self-assembling properties, mimicking viral functions and molecular organization. Naturally formed nanostructures (such as viruses, flagella or simpler protein oligomers) can be engineered to acquire specific traits of interest in biomedicine, for instance through the addition of cell targeting agents for desired biodistribution and specific delivery of associated drugs. However, fully artificial constructs would be highly desirable regarding finest tuning and adaptation to precise therapeutic purposes. Although engineering of protein assembling is still in its infancy, arising principles and promising strategies of protein manipulation point out the rational construction of nanoscale protein cages as a feasible concept, reachable through conventional recombinant DNA technologies and microbial protein production.
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spelling pubmed-30227122011-01-19 Engineering building blocks for self-assembling protein nanoparticles Vázquez, Esther Villaverde, Antonio Microb Cell Fact Commentary Like natural viruses, manmade protein cages for drug delivery are to be ideally formed by repetitive subunits with self-assembling properties, mimicking viral functions and molecular organization. Naturally formed nanostructures (such as viruses, flagella or simpler protein oligomers) can be engineered to acquire specific traits of interest in biomedicine, for instance through the addition of cell targeting agents for desired biodistribution and specific delivery of associated drugs. However, fully artificial constructs would be highly desirable regarding finest tuning and adaptation to precise therapeutic purposes. Although engineering of protein assembling is still in its infancy, arising principles and promising strategies of protein manipulation point out the rational construction of nanoscale protein cages as a feasible concept, reachable through conventional recombinant DNA technologies and microbial protein production. BioMed Central 2010-12-30 /pmc/articles/PMC3022712/ /pubmed/21192790 http://dx.doi.org/10.1186/1475-2859-9-101 Text en Copyright ©2010 Vázquez and Villaverde; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (<url>http://creativecommons.org/licenses/by/2.0</url>), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Commentary
Vázquez, Esther
Villaverde, Antonio
Engineering building blocks for self-assembling protein nanoparticles
title Engineering building blocks for self-assembling protein nanoparticles
title_full Engineering building blocks for self-assembling protein nanoparticles
title_fullStr Engineering building blocks for self-assembling protein nanoparticles
title_full_unstemmed Engineering building blocks for self-assembling protein nanoparticles
title_short Engineering building blocks for self-assembling protein nanoparticles
title_sort engineering building blocks for self-assembling protein nanoparticles
topic Commentary
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3022712/
https://www.ncbi.nlm.nih.gov/pubmed/21192790
http://dx.doi.org/10.1186/1475-2859-9-101
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