A Light Scattering Investigation of Enzymatic Gelation in Self-Assembling Peptides
Self-assembling peptides (SAPs) have been increasingly studied as hydrogel–former gelators because they can create biocompatible environments. A common strategy to trigger gelation, is to use a pH variation, but most methods result in a change in pH that is too rapid, leading to gels with hardly rep...
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| Format: | Article |
| Language: | English |
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MDPI AG
2023-04-01
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| Series: | Gels |
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| Online Access: | https://www.mdpi.com/2310-2861/9/4/347 |
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| author | Stefano Buzzaccaro Vincenzo Ruzzi Fabrizio Gelain Roberto Piazza |
| author_facet | Stefano Buzzaccaro Vincenzo Ruzzi Fabrizio Gelain Roberto Piazza |
| author_sort | Stefano Buzzaccaro |
| collection | DOAJ |
| description | Self-assembling peptides (SAPs) have been increasingly studied as hydrogel–former gelators because they can create biocompatible environments. A common strategy to trigger gelation, is to use a pH variation, but most methods result in a change in pH that is too rapid, leading to gels with hardly reproducible properties. Here, we use the urea–urease reaction to tune gel properties, by a slow and uniform pH increase. We were able to produce very homogeneous and transparent gels at several SAP concentrations, ranging from <inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><mrow><mi>c</mi><mo>=</mo><mn>1</mn><mspace width="0.166667em"></mspace><mi mathvariant="normal">g</mi><mo>/</mo><mi mathvariant="normal">L</mi></mrow></semantics></math></inline-formula> to <inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><mrow><mi>c</mi><mo>=</mo><mn>10</mn><mspace width="0.166667em"></mspace><mi mathvariant="normal">g</mi><mo>/</mo><mi mathvariant="normal">L</mi></mrow></semantics></math></inline-formula>. In addition, by exploiting such a pH control strategy, and combining photon correlation imaging with dynamic light scattering measurements, we managed to unravel the mechanism by which gelation occurs in solutions of <inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><msub><mrow><mo>(</mo><mi>LDLK</mi><mo>)</mo></mrow><mn>3</mn></msub></semantics></math></inline-formula>-based SAPs. We found that, in diluted and concentrated solutions, gelation follows different pathways. This leads to gels with different microscopic dynamics and capability of trapping nanoparticles. At high concentrations, a strong gel is formed, made of relatively thick and rigid branches that firmly entrap nanoparticles. By contrast, the gel formed in dilute conditions is weaker, characterized by entanglements and crosslinks of very thin and flexible filaments. The gel is still able to entrap nanoparticles, but their motion is not completely arrested. These different gel morphologies can potentially be exploited for controlled multiple drug release. |
| first_indexed | 2024-03-11T05:00:22Z |
| format | Article |
| id | doaj.art-ade31bde98664cd7ab34bd7b53615093 |
| institution | Directory Open Access Journal |
| issn | 2310-2861 |
| language | English |
| last_indexed | 2024-03-11T05:00:22Z |
| publishDate | 2023-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Gels |
| spelling | doaj.art-ade31bde98664cd7ab34bd7b536150932023-11-17T19:22:10ZengMDPI AGGels2310-28612023-04-019434710.3390/gels9040347A Light Scattering Investigation of Enzymatic Gelation in Self-Assembling PeptidesStefano Buzzaccaro0Vincenzo Ruzzi1Fabrizio Gelain2Roberto Piazza3Department of Chemistry, Materials Science, and Chemical Engineering (CMIC), Politecnico di Milano, Edificio 6, Piazza Leonardo da Vinci 32, 20133 Milano, ItalyDepartment of Chemistry, Materials Science, and Chemical Engineering (CMIC), Politecnico di Milano, Edificio 6, Piazza Leonardo da Vinci 32, 20133 Milano, ItalyUnità di Ingegneria Tissutale, Fondazione IRCCS Casa Sollievo della Sofferenza, 71013 San Giovanni Rotondo, ItalyDepartment of Chemistry, Materials Science, and Chemical Engineering (CMIC), Politecnico di Milano, Edificio 6, Piazza Leonardo da Vinci 32, 20133 Milano, ItalySelf-assembling peptides (SAPs) have been increasingly studied as hydrogel–former gelators because they can create biocompatible environments. A common strategy to trigger gelation, is to use a pH variation, but most methods result in a change in pH that is too rapid, leading to gels with hardly reproducible properties. Here, we use the urea–urease reaction to tune gel properties, by a slow and uniform pH increase. We were able to produce very homogeneous and transparent gels at several SAP concentrations, ranging from <inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><mrow><mi>c</mi><mo>=</mo><mn>1</mn><mspace width="0.166667em"></mspace><mi mathvariant="normal">g</mi><mo>/</mo><mi mathvariant="normal">L</mi></mrow></semantics></math></inline-formula> to <inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><mrow><mi>c</mi><mo>=</mo><mn>10</mn><mspace width="0.166667em"></mspace><mi mathvariant="normal">g</mi><mo>/</mo><mi mathvariant="normal">L</mi></mrow></semantics></math></inline-formula>. In addition, by exploiting such a pH control strategy, and combining photon correlation imaging with dynamic light scattering measurements, we managed to unravel the mechanism by which gelation occurs in solutions of <inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><msub><mrow><mo>(</mo><mi>LDLK</mi><mo>)</mo></mrow><mn>3</mn></msub></semantics></math></inline-formula>-based SAPs. We found that, in diluted and concentrated solutions, gelation follows different pathways. This leads to gels with different microscopic dynamics and capability of trapping nanoparticles. At high concentrations, a strong gel is formed, made of relatively thick and rigid branches that firmly entrap nanoparticles. By contrast, the gel formed in dilute conditions is weaker, characterized by entanglements and crosslinks of very thin and flexible filaments. The gel is still able to entrap nanoparticles, but their motion is not completely arrested. These different gel morphologies can potentially be exploited for controlled multiple drug release.https://www.mdpi.com/2310-2861/9/4/347gelsself-assembling peptidephoton correlation imagingDLSenzymatic gelation |
| spellingShingle | Stefano Buzzaccaro Vincenzo Ruzzi Fabrizio Gelain Roberto Piazza A Light Scattering Investigation of Enzymatic Gelation in Self-Assembling Peptides Gels gels self-assembling peptide photon correlation imaging DLS enzymatic gelation |
| title | A Light Scattering Investigation of Enzymatic Gelation in Self-Assembling Peptides |
| title_full | A Light Scattering Investigation of Enzymatic Gelation in Self-Assembling Peptides |
| title_fullStr | A Light Scattering Investigation of Enzymatic Gelation in Self-Assembling Peptides |
| title_full_unstemmed | A Light Scattering Investigation of Enzymatic Gelation in Self-Assembling Peptides |
| title_short | A Light Scattering Investigation of Enzymatic Gelation in Self-Assembling Peptides |
| title_sort | light scattering investigation of enzymatic gelation in self assembling peptides |
| topic | gels self-assembling peptide photon correlation imaging DLS enzymatic gelation |
| url | https://www.mdpi.com/2310-2861/9/4/347 |
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