Dimer Is Not Double: The Unexpected Behavior of Two-Floor Peptide Nanosponge

Autores
Messina, Grazia Maria Lucia; De Zotti, Marta; Siano, Alvaro Sebastían; Mazzuca, Claudia; Marletta, Giovanni; Palleschi, Antonio
Año de publicación
2024
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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.
Fil: Messina, Grazia Maria Lucia. University of Catania and Center for Colloid and Surface Science; Italia
Fil: De Zotti, Marta. Università di Padova; Italia
Fil: Siano, Alvaro Sebastían. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Química Organica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina
Fil: Mazzuca, Claudia. Universita Tor Vergata; Italia
Fil: Marletta, Giovanni. University of Catania and Center for Colloid and Surface Science; Italia
Fil: Palleschi, Antonio. Universita Tor Vergata; Italia
Materia
Dinamica Molecular
pH
Esponja Molecular
Superficies funcionalizadas
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/267085
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/267085
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Dimer Is Not Double: The Unexpected Behavior of Two-Floor Peptide NanospongeMessina, Grazia Maria LuciaDe Zotti, MartaSiano, Alvaro SebastíanMazzuca, ClaudiaMarletta, GiovanniPalleschi, AntonioDinamica MolecularpHEsponja MolecularSuperficies funcionalizadashttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Using 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.Fil: Messina, Grazia Maria Lucia. University of Catania and Center for Colloid and Surface Science; ItaliaFil: De Zotti, Marta. Università di Padova; ItaliaFil: Siano, Alvaro Sebastían. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Química Organica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; ArgentinaFil: Mazzuca, Claudia. Universita Tor Vergata; ItaliaFil: Marletta, Giovanni. University of Catania and Center for Colloid and Surface Science; ItaliaFil: Palleschi, Antonio. Universita Tor Vergata; ItaliaMolecular Diversity Preservation International2024-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/267085Messina, Grazia Maria Lucia; De Zotti, Marta; Siano, Alvaro Sebastían; Mazzuca, Claudia; Marletta, Giovanni; et al.; Dimer Is Not Double: The Unexpected Behavior of Two-Floor Peptide Nanosponge; Molecular Diversity Preservation International; Molecules; 30; 1; 12-2024; 1-171420-3049CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/1420-3049/30/1/47info:eu-repo/semantics/altIdentifier/doi/10.3390/molecules30010047info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:42:56Zoai:ri.conicet.gov.ar:11336/267085instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:42:56.319CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Dimer Is Not Double: The Unexpected Behavior of Two-Floor Peptide Nanosponge
title Dimer Is Not Double: The Unexpected Behavior of Two-Floor Peptide Nanosponge
spellingShingle Dimer Is Not Double: The Unexpected Behavior of Two-Floor Peptide Nanosponge
Messina, Grazia Maria Lucia
Dinamica Molecular
pH
Esponja Molecular
Superficies funcionalizadas
title_short 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_sort Dimer Is Not Double: The Unexpected Behavior of Two-Floor Peptide Nanosponge
dc.creator.none.fl_str_mv Messina, Grazia Maria Lucia
De Zotti, Marta
Siano, Alvaro Sebastían
Mazzuca, Claudia
Marletta, Giovanni
Palleschi, Antonio
author Messina, Grazia Maria Lucia
author_facet Messina, Grazia Maria Lucia
De Zotti, Marta
Siano, Alvaro Sebastían
Mazzuca, Claudia
Marletta, Giovanni
Palleschi, Antonio
author_role author
author2 De Zotti, Marta
Siano, Alvaro Sebastían
Mazzuca, Claudia
Marletta, Giovanni
Palleschi, Antonio
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Dinamica Molecular
pH
Esponja Molecular
Superficies funcionalizadas
topic Dinamica Molecular
pH
Esponja Molecular
Superficies funcionalizadas
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv 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.
Fil: Messina, Grazia Maria Lucia. University of Catania and Center for Colloid and Surface Science; Italia
Fil: De Zotti, Marta. Università di Padova; Italia
Fil: Siano, Alvaro Sebastían. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Química Organica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina
Fil: Mazzuca, Claudia. Universita Tor Vergata; Italia
Fil: Marletta, Giovanni. University of Catania and Center for Colloid and Surface Science; Italia
Fil: Palleschi, Antonio. Universita Tor Vergata; Italia
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.
publishDate 2024
dc.date.none.fl_str_mv 2024-12
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/267085
Messina, Grazia Maria Lucia; De Zotti, Marta; Siano, Alvaro Sebastían; Mazzuca, Claudia; Marletta, Giovanni; et al.; Dimer Is Not Double: The Unexpected Behavior of Two-Floor Peptide Nanosponge; Molecular Diversity Preservation International; Molecules; 30; 1; 12-2024; 1-17
1420-3049
CONICET Digital
CONICET
url http://hdl.handle.net/11336/267085
identifier_str_mv Messina, Grazia Maria Lucia; De Zotti, Marta; Siano, Alvaro Sebastían; Mazzuca, Claudia; Marletta, Giovanni; et al.; Dimer Is Not Double: The Unexpected Behavior of Two-Floor Peptide Nanosponge; Molecular Diversity Preservation International; Molecules; 30; 1; 12-2024; 1-17
1420-3049
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/1420-3049/30/1/47
info:eu-repo/semantics/altIdentifier/doi/10.3390/molecules30010047
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Molecular Diversity Preservation International
publisher.none.fl_str_mv Molecular Diversity Preservation International
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.070432

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