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Self-assembly/disassembly hysteresis of nanoparticles composed of marginally soluble, short elastin-like polypeptides
BACKGROUND: Elastin-like polypeptides (ELPs) are a fascinating biomaterial that has undergone copious development for a variety of therapeutic applications including as a nanoscale drug delivery vehicle. A comprehensive understanding of ELP self-assembly is lacking and this knowledge gap impedes the...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5816514/ https://www.ncbi.nlm.nih.gov/pubmed/29454362 http://dx.doi.org/10.1186/s12951-018-0342-5 |
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author | Bahniuk, Markian S. Alshememry, Abdullah K. Elgersma, Scott V. Unsworth, Larry D. |
author_facet | Bahniuk, Markian S. Alshememry, Abdullah K. Elgersma, Scott V. Unsworth, Larry D. |
author_sort | Bahniuk, Markian S. |
collection | PubMed |
description | BACKGROUND: Elastin-like polypeptides (ELPs) are a fascinating biomaterial that has undergone copious development for a variety of therapeutic applications including as a nanoscale drug delivery vehicle. A comprehensive understanding of ELP self-assembly is lacking and this knowledge gap impedes the advancement of ELP-based biomaterials into the clinical realm. The systematic examination of leucine-containing ELPs endeavors to expand existing knowledge about fundamental assembly–disassembly behaviours. RESULTS: It was observed that these marginally soluble, short ELPs tend to behave consistently with previous observations related to assembly-related ELP phase transitions but deviated in their disassembly. It was found that chain length, concentration and overall sequence hydrophobicity may influence the irreversible formation of sub-micron particles as well as the formation of multi-micron scale, colloidally unstable aggregates. Amino acid composition affected surface charge and packing density of the particles. Particle stability upon dilution was found to vary depending upon chain length and hydrophobicity, with particles composed of longer and/or more hydrophobic ELPs being more resistant to disassembly upon isothermal dilution. CONCLUSIONS: Taken together, these results suggest marginally soluble ELPs may self-assemble but not disassemble as expected and that parameters including particle size, zeta potential and dilution resistance would benefit from widespread systematic evaluations. This information has the potential to reveal novel preparation methods capable of expanding the utility of all existing ELP-based biomaterials. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s12951-018-0342-5) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-5816514 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-58165142018-02-21 Self-assembly/disassembly hysteresis of nanoparticles composed of marginally soluble, short elastin-like polypeptides Bahniuk, Markian S. Alshememry, Abdullah K. Elgersma, Scott V. Unsworth, Larry D. J Nanobiotechnology Research BACKGROUND: Elastin-like polypeptides (ELPs) are a fascinating biomaterial that has undergone copious development for a variety of therapeutic applications including as a nanoscale drug delivery vehicle. A comprehensive understanding of ELP self-assembly is lacking and this knowledge gap impedes the advancement of ELP-based biomaterials into the clinical realm. The systematic examination of leucine-containing ELPs endeavors to expand existing knowledge about fundamental assembly–disassembly behaviours. RESULTS: It was observed that these marginally soluble, short ELPs tend to behave consistently with previous observations related to assembly-related ELP phase transitions but deviated in their disassembly. It was found that chain length, concentration and overall sequence hydrophobicity may influence the irreversible formation of sub-micron particles as well as the formation of multi-micron scale, colloidally unstable aggregates. Amino acid composition affected surface charge and packing density of the particles. Particle stability upon dilution was found to vary depending upon chain length and hydrophobicity, with particles composed of longer and/or more hydrophobic ELPs being more resistant to disassembly upon isothermal dilution. CONCLUSIONS: Taken together, these results suggest marginally soluble ELPs may self-assemble but not disassemble as expected and that parameters including particle size, zeta potential and dilution resistance would benefit from widespread systematic evaluations. This information has the potential to reveal novel preparation methods capable of expanding the utility of all existing ELP-based biomaterials. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s12951-018-0342-5) contains supplementary material, which is available to authorized users. BioMed Central 2018-02-17 /pmc/articles/PMC5816514/ /pubmed/29454362 http://dx.doi.org/10.1186/s12951-018-0342-5 Text en © The Author(s) 2018 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. 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 | Research Bahniuk, Markian S. Alshememry, Abdullah K. Elgersma, Scott V. Unsworth, Larry D. Self-assembly/disassembly hysteresis of nanoparticles composed of marginally soluble, short elastin-like polypeptides |
title | Self-assembly/disassembly hysteresis of nanoparticles composed of marginally soluble, short elastin-like polypeptides |
title_full | Self-assembly/disassembly hysteresis of nanoparticles composed of marginally soluble, short elastin-like polypeptides |
title_fullStr | Self-assembly/disassembly hysteresis of nanoparticles composed of marginally soluble, short elastin-like polypeptides |
title_full_unstemmed | Self-assembly/disassembly hysteresis of nanoparticles composed of marginally soluble, short elastin-like polypeptides |
title_short | Self-assembly/disassembly hysteresis of nanoparticles composed of marginally soluble, short elastin-like polypeptides |
title_sort | self-assembly/disassembly hysteresis of nanoparticles composed of marginally soluble, short elastin-like polypeptides |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5816514/ https://www.ncbi.nlm.nih.gov/pubmed/29454362 http://dx.doi.org/10.1186/s12951-018-0342-5 |
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