Dimer Is Not Double: The Unexpected Behavior of Two-Floor Peptide Nanosponge
Using the framework of an investigation of the stimuli-responsive behavior of peptide assembly on a solid surface, this study on the behavior of a chemisorbed peptide on a gold surface was performed. The studied peptide is a dimeric form of the antimicrobial peptide Trichogin GAIV, which was also mo...
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2024-12-01
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| author | Grazia Maria Lucia Messina Marta De Zotti Alvaro S. Siano Claudia Mazzuca Giovanni Marletta Antonio Palleschi |
| author_facet | Grazia Maria Lucia Messina Marta De Zotti Alvaro S. Siano Claudia Mazzuca Giovanni Marletta Antonio Palleschi |
| author_sort | Grazia Maria Lucia Messina |
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| description | Using the framework of an investigation of the stimuli-responsive behavior of peptide assembly on a solid surface, this study on the behavior of a chemisorbed peptide on a gold surface was performed. The studied peptide is a dimeric form of the antimicrobial peptide Trichogin GAIV, which was also modified by substituting the glycine with lysine residues, while the N-terminus octanoyl group was replaced by a lipoic one that was able to bind to the gold surface. In this way, a chemically linked peptide assembly that is pH-responsive was obtained because of the protonation/deprotonation of the sidechains of the Lys residues. Information about the effect of protonation/deprotonation equilibria switching the pH from acid (pH = 3) to basic (pH = 11) conditions was obtained macroscopically by performing Quartz crystal microbalance with dissipation monitoring (QCM-D), Surface Plasmon Resonance (SPR), Nanoplasmonic Sensing (NPS), and FTIR techniques. Using molecular dynamics (MD) simulations, it is possible to explain, at the molecular level, our main experimental results: (1) pH changes induce a squeezing behavior in the system, consisting in thickness and mass variations in the peptide layer, which are mainly due to the pH-driven hydrophilic/hydrophobic character of the lysine residues, and (2) the observed hysteresis is due to small conformational rearrangements from helix to beta sheets occurring mainly on the first half of the peptide, closer to the surface, while the second half remains almost unaffected. The latter result, together with the evidence that the layer thickness is not simply double the assembly of the monomeric analog, indicates that the dimeric peptide does not behave as a double monomer, but assumes very peculiar features. |
| format | Article |
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| institution | Kabale University |
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| language | English |
| publishDate | 2024-12-01 |
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| series | Molecules |
| spelling | doaj-art-6fe49028884e43ba93e866382a671fe72025-01-10T13:18:43ZengMDPI AGMolecules1420-30492024-12-013014710.3390/molecules30010047Dimer Is Not Double: The Unexpected Behavior of Two-Floor Peptide NanospongeGrazia Maria Lucia Messina0Marta De Zotti1Alvaro S. Siano2Claudia Mazzuca3Giovanni Marletta4Antonio Palleschi5Laboratory for Molecular Surfaces and Nanotechnology (LAMSUN), Department of Chemical Sciences, University of Catania and Center for Colloid and Surface Science (CSGI), Viale A. Doria 6, 95125 Catania, ItalyDepartment of Chemical Sciences, University of Padua, Via Marzolo 1, 35131 Padua, ItalyLaboratorio de Peptidos Bioactivos (LPB), Departamento de Química Organica, Facultad de Bioquímica y Ciencias Biologicas (FBCB), Universidad Nacional del Litoral (UNL), Santa Fe 3000, ArgentinaDepartment of Chemical Science and Technologies, University of Rome “Tor Vergata”, Via della Ricerca Scientifica, 00133 Rome, ItalyLaboratory for Molecular Surfaces and Nanotechnology, (LAMSUN), Center for Colloid and Surface Science (CSGI), Viale A. Doria 6, 95125 Catania, ItalyDepartment of Chemical Science and Technologies, University of Rome “Tor Vergata”, Via della Ricerca Scientifica, 00133 Rome, ItalyUsing the framework of an investigation of the stimuli-responsive behavior of peptide assembly on a solid surface, this study on the behavior of a chemisorbed peptide on a gold surface was performed. The studied peptide is a dimeric form of the antimicrobial peptide Trichogin GAIV, which was also modified by substituting the glycine with lysine residues, while the N-terminus octanoyl group was replaced by a lipoic one that was able to bind to the gold surface. In this way, a chemically linked peptide assembly that is pH-responsive was obtained because of the protonation/deprotonation of the sidechains of the Lys residues. Information about the effect of protonation/deprotonation equilibria switching the pH from acid (pH = 3) to basic (pH = 11) conditions was obtained macroscopically by performing Quartz crystal microbalance with dissipation monitoring (QCM-D), Surface Plasmon Resonance (SPR), Nanoplasmonic Sensing (NPS), and FTIR techniques. Using molecular dynamics (MD) simulations, it is possible to explain, at the molecular level, our main experimental results: (1) pH changes induce a squeezing behavior in the system, consisting in thickness and mass variations in the peptide layer, which are mainly due to the pH-driven hydrophilic/hydrophobic character of the lysine residues, and (2) the observed hysteresis is due to small conformational rearrangements from helix to beta sheets occurring mainly on the first half of the peptide, closer to the surface, while the second half remains almost unaffected. The latter result, together with the evidence that the layer thickness is not simply double the assembly of the monomeric analog, indicates that the dimeric peptide does not behave as a double monomer, but assumes very peculiar features.https://www.mdpi.com/1420-3049/30/1/47peptide assemblypH external stimuliQCM-Dmolecular dynamic simulationfunctionalized surfacemolecular sponge |
| spellingShingle | Grazia Maria Lucia Messina Marta De Zotti Alvaro S. Siano Claudia Mazzuca Giovanni Marletta Antonio Palleschi Dimer Is Not Double: The Unexpected Behavior of Two-Floor Peptide Nanosponge Molecules peptide assembly pH external stimuli QCM-D molecular dynamic simulation functionalized surface molecular sponge |
| title | Dimer Is Not Double: The Unexpected Behavior of Two-Floor Peptide Nanosponge |
| title_full | Dimer Is Not Double: The Unexpected Behavior of Two-Floor Peptide Nanosponge |
| title_fullStr | Dimer Is Not Double: The Unexpected Behavior of Two-Floor Peptide Nanosponge |
| title_full_unstemmed | Dimer Is Not Double: The Unexpected Behavior of Two-Floor Peptide Nanosponge |
| title_short | Dimer Is Not Double: The Unexpected Behavior of Two-Floor Peptide Nanosponge |
| title_sort | dimer is not double the unexpected behavior of two floor peptide nanosponge |
| topic | peptide assembly pH external stimuli QCM-D molecular dynamic simulation functionalized surface molecular sponge |
| url | https://www.mdpi.com/1420-3049/30/1/47 |
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