Influence of Electrostatic Interactions on the Self-Assembly of Charged Peptides
Peptides can be designed to self-assemble into predefined supramolecular nanostructures, which are then employed as biomaterials in a range of applications, including tissue engineering, drug delivery, and vaccination. However, current self-assembling peptide (SAP) hydrogels exhibit inadequate self-...
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MDPI AG
2025-01-01
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author | Xue Sun Bolan Wu Na Li Bo Liu Shijun Li Liang Ma Hangyu Zhang |
author_facet | Xue Sun Bolan Wu Na Li Bo Liu Shijun Li Liang Ma Hangyu Zhang |
author_sort | Xue Sun |
collection | DOAJ |
description | Peptides can be designed to self-assemble into predefined supramolecular nanostructures, which are then employed as biomaterials in a range of applications, including tissue engineering, drug delivery, and vaccination. However, current self-assembling peptide (SAP) hydrogels exhibit inadequate self-healing capacities and necessitate the use of sophisticated printing apparatus, rendering them unsuitable for 3D printing under physiological conditions. Here, we report a precisely designed charged peptide, Z5, with the object of investigating the impact of electrostatic interactions on the self-assembly and the rheological properties of the resulting hydrogels. This peptide displays salt-triggered self-assembly resulting in the formation of a nanofiber network with a high β-sheet content. The peptide self-assembly and the hydrogel properties can be modified according to the ionic environment. It is noteworthy that the Z5 hydrogel in normal saline (NS) shows exceptional self-healing properties, demonstrating the ability to recover its initial strength in seconds after the removal of shear force, thus rendering it an acceptable material for printing. In contrast, the strong salt shielding effect and the ionic cross-linking of Z5 hydrogels in PBS result in the bundling of peptide nanofibers, which impedes the recovery of the initial strength post-destruction. Furthermore, incorporating materials with varied charging properties into Z5 hydrogels can alter the electrostatic interactions among peptide nanofibers, further modulating the rheological properties and the printability of SAP hydrogels. |
format | Article |
id | doaj-art-555def5cb5d04d598645a81cabfa3108 |
institution | Kabale University |
issn | 2310-2861 |
language | English |
publishDate | 2025-01-01 |
publisher | MDPI AG |
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series | Gels |
spelling | doaj-art-555def5cb5d04d598645a81cabfa31082025-01-24T13:34:04ZengMDPI AGGels2310-28612025-01-011118010.3390/gels11010080Influence of Electrostatic Interactions on the Self-Assembly of Charged PeptidesXue Sun0Bolan Wu1Na Li2Bo Liu3Shijun Li4Liang Ma5Hangyu Zhang6Faculty of Medicine, Dalian University of Technology, Dalian 116033, ChinaLiaoning Key Lab of Integrated Circuit and Biomedical Electronic System, School of Biomedical Engineering, Dalian University of Technology, Dalian 116024, ChinaLiaoning Key Lab of Integrated Circuit and Biomedical Electronic System, School of Biomedical Engineering, Dalian University of Technology, Dalian 116024, ChinaLiaoning Key Lab of Integrated Circuit and Biomedical Electronic System, School of Biomedical Engineering, Dalian University of Technology, Dalian 116024, ChinaFaculty of Medicine, Dalian University of Technology, Dalian 116033, ChinaFaculty of Medicine, Dalian University of Technology, Dalian 116033, ChinaFaculty of Medicine, Dalian University of Technology, Dalian 116033, ChinaPeptides can be designed to self-assemble into predefined supramolecular nanostructures, which are then employed as biomaterials in a range of applications, including tissue engineering, drug delivery, and vaccination. However, current self-assembling peptide (SAP) hydrogels exhibit inadequate self-healing capacities and necessitate the use of sophisticated printing apparatus, rendering them unsuitable for 3D printing under physiological conditions. Here, we report a precisely designed charged peptide, Z5, with the object of investigating the impact of electrostatic interactions on the self-assembly and the rheological properties of the resulting hydrogels. This peptide displays salt-triggered self-assembly resulting in the formation of a nanofiber network with a high β-sheet content. The peptide self-assembly and the hydrogel properties can be modified according to the ionic environment. It is noteworthy that the Z5 hydrogel in normal saline (NS) shows exceptional self-healing properties, demonstrating the ability to recover its initial strength in seconds after the removal of shear force, thus rendering it an acceptable material for printing. In contrast, the strong salt shielding effect and the ionic cross-linking of Z5 hydrogels in PBS result in the bundling of peptide nanofibers, which impedes the recovery of the initial strength post-destruction. Furthermore, incorporating materials with varied charging properties into Z5 hydrogels can alter the electrostatic interactions among peptide nanofibers, further modulating the rheological properties and the printability of SAP hydrogels.https://www.mdpi.com/2310-2861/11/1/80self-assembling peptideelectrostatic interactions3D printinghydrogelself-healing |
spellingShingle | Xue Sun Bolan Wu Na Li Bo Liu Shijun Li Liang Ma Hangyu Zhang Influence of Electrostatic Interactions on the Self-Assembly of Charged Peptides Gels self-assembling peptide electrostatic interactions 3D printing hydrogel self-healing |
title | Influence of Electrostatic Interactions on the Self-Assembly of Charged Peptides |
title_full | Influence of Electrostatic Interactions on the Self-Assembly of Charged Peptides |
title_fullStr | Influence of Electrostatic Interactions on the Self-Assembly of Charged Peptides |
title_full_unstemmed | Influence of Electrostatic Interactions on the Self-Assembly of Charged Peptides |
title_short | Influence of Electrostatic Interactions on the Self-Assembly of Charged Peptides |
title_sort | influence of electrostatic interactions on the self assembly of charged peptides |
topic | self-assembling peptide electrostatic interactions 3D printing hydrogel self-healing |
url | https://www.mdpi.com/2310-2861/11/1/80 |
work_keys_str_mv | AT xuesun influenceofelectrostaticinteractionsontheselfassemblyofchargedpeptides AT bolanwu influenceofelectrostaticinteractionsontheselfassemblyofchargedpeptides AT nali influenceofelectrostaticinteractionsontheselfassemblyofchargedpeptides AT boliu influenceofelectrostaticinteractionsontheselfassemblyofchargedpeptides AT shijunli influenceofelectrostaticinteractionsontheselfassemblyofchargedpeptides AT liangma influenceofelectrostaticinteractionsontheselfassemblyofchargedpeptides AT hangyuzhang influenceofelectrostaticinteractionsontheselfassemblyofchargedpeptides |