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Directed self-assembly of proteins into discrete radial patterns
Unlike physical patterning of materials at nanometer scale, manipulating soft matter such as biomolecules into patterns is still in its infancy. Self-assembled monolayer (SAM) with surface density gradient has the capability to drive biomolecules in specific directions to create hierarchical and dis...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3667488/ https://www.ncbi.nlm.nih.gov/pubmed/23719678 http://dx.doi.org/10.1038/srep01923 |
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author | Thakur, Garima Prashanthi, Kovur Thundat, Thomas |
author_facet | Thakur, Garima Prashanthi, Kovur Thundat, Thomas |
author_sort | Thakur, Garima |
collection | PubMed |
description | Unlike physical patterning of materials at nanometer scale, manipulating soft matter such as biomolecules into patterns is still in its infancy. Self-assembled monolayer (SAM) with surface density gradient has the capability to drive biomolecules in specific directions to create hierarchical and discrete structures. Here, we report on a two-step process of self-assembly of the human serum albumin (HSA) protein into discrete ring structures based on density gradient of SAM. The methodology involves first creating a 2-dimensional (2D) polyethylene glycol (PEG) islands with responsive carboxyl functionalities. Incubation of proteins on such pre-patterned surfaces results in direct self-assembly of protein molecules around PEG islands. Immobilization and adsorption of protein on such structures over time evolve into the self-assembled patterns. |
format | Online Article Text |
id | pubmed-3667488 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-36674882013-05-30 Directed self-assembly of proteins into discrete radial patterns Thakur, Garima Prashanthi, Kovur Thundat, Thomas Sci Rep Article Unlike physical patterning of materials at nanometer scale, manipulating soft matter such as biomolecules into patterns is still in its infancy. Self-assembled monolayer (SAM) with surface density gradient has the capability to drive biomolecules in specific directions to create hierarchical and discrete structures. Here, we report on a two-step process of self-assembly of the human serum albumin (HSA) protein into discrete ring structures based on density gradient of SAM. The methodology involves first creating a 2-dimensional (2D) polyethylene glycol (PEG) islands with responsive carboxyl functionalities. Incubation of proteins on such pre-patterned surfaces results in direct self-assembly of protein molecules around PEG islands. Immobilization and adsorption of protein on such structures over time evolve into the self-assembled patterns. Nature Publishing Group 2013-05-30 /pmc/articles/PMC3667488/ /pubmed/23719678 http://dx.doi.org/10.1038/srep01923 Text en Copyright © 2013, Macmillan Publishers Limited. All rights reserved http://creativecommons.org/licenses/by-nc-nd/3.0/ This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-nd/3.0/ |
spellingShingle | Article Thakur, Garima Prashanthi, Kovur Thundat, Thomas Directed self-assembly of proteins into discrete radial patterns |
title | Directed self-assembly of proteins into discrete radial patterns |
title_full | Directed self-assembly of proteins into discrete radial patterns |
title_fullStr | Directed self-assembly of proteins into discrete radial patterns |
title_full_unstemmed | Directed self-assembly of proteins into discrete radial patterns |
title_short | Directed self-assembly of proteins into discrete radial patterns |
title_sort | directed self-assembly of proteins into discrete radial patterns |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3667488/ https://www.ncbi.nlm.nih.gov/pubmed/23719678 http://dx.doi.org/10.1038/srep01923 |
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