Modulating the poly-l-lysine structure through the control of the protonation–deprotonation state of l-lysine
Abstract Designing the architecture of l-lysine-based polymeric structures is a highly challenging task that requires careful control of the amino acid reactive groups. Conventional processes to obtain branched polylysine need several steps and the addition of specific catalysts. In the present work...
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2022-11-01
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| Series: | Scientific Reports |
| Online Access: | https://doi.org/10.1038/s41598-022-24109-5 |
| _version_ | 1811319592053637120 |
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| author | Luigi Stagi Martina Sini Davide Carboni Roberto Anedda Giuliano Siligardi Tiberiu-Marius Gianga Rohanah Hussain Plinio Innocenzi |
| author_facet | Luigi Stagi Martina Sini Davide Carboni Roberto Anedda Giuliano Siligardi Tiberiu-Marius Gianga Rohanah Hussain Plinio Innocenzi |
| author_sort | Luigi Stagi |
| collection | DOAJ |
| description | Abstract Designing the architecture of l-lysine-based polymeric structures is a highly challenging task that requires careful control of the amino acid reactive groups. Conventional processes to obtain branched polylysine need several steps and the addition of specific catalysts. In the present work, to gain a better understanding and control of the formation of l-lysine-based polymers, we have investigated the correlation between the protonation state of l-lysine and the corresponding hydrothermally grown structures. The samples have been characterized by combining optical spectroscopies, such as UV–Vis, fluorescence, and synchrotron radiation circular dichroism with structural analysis by Nuclear Magnetic Resonance, Fourier Transform Infrared spectroscopy, and dynamic light scattering. We have observed that aqueous precursor solutions with alkaline pHs promote the formation of branched structures. In contrast, high pHs favour the reactivity of the ε-amino groups leading to linear structures, as shown by circular dichroism analyses. On the other hand, acidic conditions trigger the branching of the amino acid. Interestingly, the polymeric forms of l-lysine emit in the blue because the increasing number of intermolecular hydrogen bonds promote the intermolecular charge transfer responsible for the emission. Understanding the correlation between the l-lysine charged states and the polymeric structures that could form controlling the protonation–deprotonation states of the amino acid opens the route to a refined design of polypeptide systems based on l-lysine. |
| first_indexed | 2024-04-13T12:45:41Z |
| format | Article |
| id | doaj.art-842eb23c685640da811a94b51a836301 |
| institution | Directory Open Access Journal |
| issn | 2045-2322 |
| language | English |
| last_indexed | 2024-04-13T12:45:41Z |
| publishDate | 2022-11-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj.art-842eb23c685640da811a94b51a8363012022-12-22T02:46:22ZengNature PortfolioScientific Reports2045-23222022-11-0112111310.1038/s41598-022-24109-5Modulating the poly-l-lysine structure through the control of the protonation–deprotonation state of l-lysineLuigi Stagi0Martina Sini1Davide Carboni2Roberto Anedda3Giuliano Siligardi4Tiberiu-Marius Gianga5Rohanah Hussain6Plinio Innocenzi7Department of Chemistry, Physics, Mathematics and Natural Sciences, University of SassariLaboratory of Materials Science and Nanotechnology (LMNT), Department of Biomedical Sciences, CR-INSTM, University of SassariLaboratory of Materials Science and Nanotechnology (LMNT), Department of Biomedical Sciences, CR-INSTM, University of SassariPorto Conte RicercheDiamond Light Source Ltd., Harwell Science and Innovation CampusDiamond Light Source Ltd., Harwell Science and Innovation CampusDiamond Light Source Ltd., Harwell Science and Innovation CampusLaboratory of Materials Science and Nanotechnology (LMNT), Department of Biomedical Sciences, CR-INSTM, University of SassariAbstract Designing the architecture of l-lysine-based polymeric structures is a highly challenging task that requires careful control of the amino acid reactive groups. Conventional processes to obtain branched polylysine need several steps and the addition of specific catalysts. In the present work, to gain a better understanding and control of the formation of l-lysine-based polymers, we have investigated the correlation between the protonation state of l-lysine and the corresponding hydrothermally grown structures. The samples have been characterized by combining optical spectroscopies, such as UV–Vis, fluorescence, and synchrotron radiation circular dichroism with structural analysis by Nuclear Magnetic Resonance, Fourier Transform Infrared spectroscopy, and dynamic light scattering. We have observed that aqueous precursor solutions with alkaline pHs promote the formation of branched structures. In contrast, high pHs favour the reactivity of the ε-amino groups leading to linear structures, as shown by circular dichroism analyses. On the other hand, acidic conditions trigger the branching of the amino acid. Interestingly, the polymeric forms of l-lysine emit in the blue because the increasing number of intermolecular hydrogen bonds promote the intermolecular charge transfer responsible for the emission. Understanding the correlation between the l-lysine charged states and the polymeric structures that could form controlling the protonation–deprotonation states of the amino acid opens the route to a refined design of polypeptide systems based on l-lysine.https://doi.org/10.1038/s41598-022-24109-5 |
| spellingShingle | Luigi Stagi Martina Sini Davide Carboni Roberto Anedda Giuliano Siligardi Tiberiu-Marius Gianga Rohanah Hussain Plinio Innocenzi Modulating the poly-l-lysine structure through the control of the protonation–deprotonation state of l-lysine Scientific Reports |
| title | Modulating the poly-l-lysine structure through the control of the protonation–deprotonation state of l-lysine |
| title_full | Modulating the poly-l-lysine structure through the control of the protonation–deprotonation state of l-lysine |
| title_fullStr | Modulating the poly-l-lysine structure through the control of the protonation–deprotonation state of l-lysine |
| title_full_unstemmed | Modulating the poly-l-lysine structure through the control of the protonation–deprotonation state of l-lysine |
| title_short | Modulating the poly-l-lysine structure through the control of the protonation–deprotonation state of l-lysine |
| title_sort | modulating the poly l lysine structure through the control of the protonation deprotonation state of l lysine |
| url | https://doi.org/10.1038/s41598-022-24109-5 |
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