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Controlling the Self-Assembly and Material Properties of β-Sheet Peptide Hydrogels by Modulating Intermolecular Interactions

Self-assembling peptides are a promising biomaterial with potential applications in medical devices and drug delivery. In the right combination of conditions, self-assembling peptides can form self-supporting hydrogels. Here, we describe how balancing attractive and repulsive intermolecular forces i...

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Autores principales: Warren, James P., Culbert, Matthew P., Miles, Danielle E., Maude, Steven, Wilcox, Ruth K., Beales, Paul A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10297975/
https://www.ncbi.nlm.nih.gov/pubmed/37367112
http://dx.doi.org/10.3390/gels9060441
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author Warren, James P.
Culbert, Matthew P.
Miles, Danielle E.
Maude, Steven
Wilcox, Ruth K.
Beales, Paul A.
author_facet Warren, James P.
Culbert, Matthew P.
Miles, Danielle E.
Maude, Steven
Wilcox, Ruth K.
Beales, Paul A.
author_sort Warren, James P.
collection PubMed
description Self-assembling peptides are a promising biomaterial with potential applications in medical devices and drug delivery. In the right combination of conditions, self-assembling peptides can form self-supporting hydrogels. Here, we describe how balancing attractive and repulsive intermolecular forces is critical for successful hydrogel formation. Electrostatic repulsion is tuned by altering the peptide’s net charge, and intermolecular attractions are controlled through the degree of hydrogen bonding between specific amino acid residues. We find that an overall net peptide charge of +/−2 is optimal to facilitate the assembly of self-supporting hydrogels. If the net peptide charge is too low then dense aggregates form, while a high molecular charge inhibits the formation of larger structures. At a constant charge, altering the terminal amino acids from glutamine to serine decreases the degree of hydrogen bonding within the assembling network. This tunes the viscoelastic properties of the gel, reducing the elastic modulus by two to three orders of magnitude. Finally, hydrogels could be formed from glutamine-rich, highly charged peptides by mixing the peptides in combinations with a resultant net charge of +/−2. These results illustrate how understanding and controlling self-assembly mechanisms through modulating intermolecular interactions can be exploited to derive a range of structures with tuneable properties.
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spelling pubmed-102979752023-06-28 Controlling the Self-Assembly and Material Properties of β-Sheet Peptide Hydrogels by Modulating Intermolecular Interactions Warren, James P. Culbert, Matthew P. Miles, Danielle E. Maude, Steven Wilcox, Ruth K. Beales, Paul A. Gels Article Self-assembling peptides are a promising biomaterial with potential applications in medical devices and drug delivery. In the right combination of conditions, self-assembling peptides can form self-supporting hydrogels. Here, we describe how balancing attractive and repulsive intermolecular forces is critical for successful hydrogel formation. Electrostatic repulsion is tuned by altering the peptide’s net charge, and intermolecular attractions are controlled through the degree of hydrogen bonding between specific amino acid residues. We find that an overall net peptide charge of +/−2 is optimal to facilitate the assembly of self-supporting hydrogels. If the net peptide charge is too low then dense aggregates form, while a high molecular charge inhibits the formation of larger structures. At a constant charge, altering the terminal amino acids from glutamine to serine decreases the degree of hydrogen bonding within the assembling network. This tunes the viscoelastic properties of the gel, reducing the elastic modulus by two to three orders of magnitude. Finally, hydrogels could be formed from glutamine-rich, highly charged peptides by mixing the peptides in combinations with a resultant net charge of +/−2. These results illustrate how understanding and controlling self-assembly mechanisms through modulating intermolecular interactions can be exploited to derive a range of structures with tuneable properties. MDPI 2023-05-26 /pmc/articles/PMC10297975/ /pubmed/37367112 http://dx.doi.org/10.3390/gels9060441 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Warren, James P.
Culbert, Matthew P.
Miles, Danielle E.
Maude, Steven
Wilcox, Ruth K.
Beales, Paul A.
Controlling the Self-Assembly and Material Properties of β-Sheet Peptide Hydrogels by Modulating Intermolecular Interactions
title Controlling the Self-Assembly and Material Properties of β-Sheet Peptide Hydrogels by Modulating Intermolecular Interactions
title_full Controlling the Self-Assembly and Material Properties of β-Sheet Peptide Hydrogels by Modulating Intermolecular Interactions
title_fullStr Controlling the Self-Assembly and Material Properties of β-Sheet Peptide Hydrogels by Modulating Intermolecular Interactions
title_full_unstemmed Controlling the Self-Assembly and Material Properties of β-Sheet Peptide Hydrogels by Modulating Intermolecular Interactions
title_short Controlling the Self-Assembly and Material Properties of β-Sheet Peptide Hydrogels by Modulating Intermolecular Interactions
title_sort controlling the self-assembly and material properties of β-sheet peptide hydrogels by modulating intermolecular interactions
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10297975/
https://www.ncbi.nlm.nih.gov/pubmed/37367112
http://dx.doi.org/10.3390/gels9060441
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