pH-Responsive Capsules with a Fibril Scaffold Shell Assembled from an Amyloidogenic Peptide
(2021) In Small 17(26).- Abstract
Peptides and proteins have evolved to self-assemble into supramolecular entities through a set of non-covalent interactions. Such structures and materials provide the functional basis of life. Crucially, biomolecular assembly processes can be highly sensitive to and modulated by environmental conditions, including temperature, light, ionic strength and pH, providing the inspiration for the development of new classes of responsive functional materials based on peptide building blocks. Here, it is shown that the stimuli-responsive assembly of amyloidogenic peptide can be used as the basis of environmentally responsive microcapsules which exhibit release characteristics triggered by a change in pH. The microcapsules are biocompatible and... (More)
Peptides and proteins have evolved to self-assemble into supramolecular entities through a set of non-covalent interactions. Such structures and materials provide the functional basis of life. Crucially, biomolecular assembly processes can be highly sensitive to and modulated by environmental conditions, including temperature, light, ionic strength and pH, providing the inspiration for the development of new classes of responsive functional materials based on peptide building blocks. Here, it is shown that the stimuli-responsive assembly of amyloidogenic peptide can be used as the basis of environmentally responsive microcapsules which exhibit release characteristics triggered by a change in pH. The microcapsules are biocompatible and biodegradable and may act as vehicles for controlled release of a wide range of biomolecules. Cryo-SEM images reveal the formation of a fibrillar network of the capsule interior with discrete compartments in which cargo molecules can be stored. In addition, the reversible formation of these microcapsules by modulating the solution pH is investigated and their potential application for the controlled release of encapsulated cargo molecules, including antibodies, is shown. These results suggest that the approach described here represents a promising venue for generating pH-responsive functional peptide-based materials for a wide range of potential applications for molecular encapsulation, storage, and release.
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- author
- Shimanovich, Ulyana ; Levin, Aviad ; Eliaz, Dror ; Michaels, Thomas ; Toprakcioglu, Zenon ; Frohm, Birgitta LU ; De Genst, Erwin ; Linse, Sara LU ; Åkerfeldt, Karin S. LU and Knowles, Tuomas P.J.
- organization
- publishing date
- 2021
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- amyloid, capsule, fibrillar protein self-assembly, microfluidics, pH-responsive peptide
- in
- Small
- volume
- 17
- issue
- 26
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- pmid:34050722
- scopus:85106695978
- ISSN
- 1613-6810
- DOI
- 10.1002/smll.202007188
- language
- English
- LU publication?
- yes
- id
- c80abab0-73fe-4fd3-9e48-176aa0e0393e
- date added to LUP
- 2021-06-14 10:20:20
- date last changed
- 2024-04-20 07:25:29
@article{c80abab0-73fe-4fd3-9e48-176aa0e0393e,
abstract = {{<p>Peptides and proteins have evolved to self-assemble into supramolecular entities through a set of non-covalent interactions. Such structures and materials provide the functional basis of life. Crucially, biomolecular assembly processes can be highly sensitive to and modulated by environmental conditions, including temperature, light, ionic strength and pH, providing the inspiration for the development of new classes of responsive functional materials based on peptide building blocks. Here, it is shown that the stimuli-responsive assembly of amyloidogenic peptide can be used as the basis of environmentally responsive microcapsules which exhibit release characteristics triggered by a change in pH. The microcapsules are biocompatible and biodegradable and may act as vehicles for controlled release of a wide range of biomolecules. Cryo-SEM images reveal the formation of a fibrillar network of the capsule interior with discrete compartments in which cargo molecules can be stored. In addition, the reversible formation of these microcapsules by modulating the solution pH is investigated and their potential application for the controlled release of encapsulated cargo molecules, including antibodies, is shown. These results suggest that the approach described here represents a promising venue for generating pH-responsive functional peptide-based materials for a wide range of potential applications for molecular encapsulation, storage, and release.</p>}},
author = {{Shimanovich, Ulyana and Levin, Aviad and Eliaz, Dror and Michaels, Thomas and Toprakcioglu, Zenon and Frohm, Birgitta and De Genst, Erwin and Linse, Sara and Åkerfeldt, Karin S. and Knowles, Tuomas P.J.}},
issn = {{1613-6810}},
keywords = {{amyloid; capsule; fibrillar protein self-assembly; microfluidics; pH-responsive peptide}},
language = {{eng}},
number = {{26}},
publisher = {{John Wiley & Sons Inc.}},
series = {{Small}},
title = {{pH-Responsive Capsules with a Fibril Scaffold Shell Assembled from an Amyloidogenic Peptide}},
url = {{http://dx.doi.org/10.1002/smll.202007188}},
doi = {{10.1002/smll.202007188}},
volume = {{17}},
year = {{2021}},
}