Cargando…

From nanoaggregates to mesoscale ribbons: the multistep self-organization of amphiphilic peptides

This paper reports atomic force microscopy results and molecular dynamics simulations of the striking differences of long-term self-organization structures of negatively charged (AcA(4))(2)KD (double tail) and AcA(4)D (single tail) peptides, respectively, forming micrometer-long, linearly ordered ri...

Descripción completa

Detalles Bibliográficos
Autores principales: Messina, Grazia M. L., Mazzuca, Claudia, Dettin, Monica, Zamuner, Annj, Di Napoli, Benedetta, Ripani, Giorgio, Marletta, Giovanni, Palleschi, Antonio
Formato: Online Artículo Texto
Lenguaje:English
Publicado: RSC 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9418424/
https://www.ncbi.nlm.nih.gov/pubmed/36133720
http://dx.doi.org/10.1039/d1na00216c
_version_ 1784776941268631552
author Messina, Grazia M. L.
Mazzuca, Claudia
Dettin, Monica
Zamuner, Annj
Di Napoli, Benedetta
Ripani, Giorgio
Marletta, Giovanni
Palleschi, Antonio
author_facet Messina, Grazia M. L.
Mazzuca, Claudia
Dettin, Monica
Zamuner, Annj
Di Napoli, Benedetta
Ripani, Giorgio
Marletta, Giovanni
Palleschi, Antonio
author_sort Messina, Grazia M. L.
collection PubMed
description This paper reports atomic force microscopy results and molecular dynamics simulations of the striking differences of long-term self-organization structures of negatively charged (AcA(4))(2)KD (double tail) and AcA(4)D (single tail) peptides, respectively, forming micrometer-long, linearly ordered ribbon-like structures and nanometer-sized, unstructured, round-shaped aggregates. The subsequent formation steps of the long-range nanoribbons, experimentally observed only for the “double tail” (AcA(4))(2)KD peptide, are analyzed in detail, showing that the initial “primary” unstructured round-shaped aggregates progressively evolve into longer nanofilaments and into micrometer-long, network-forming nanoribbon moieties. In particular, the long-range self-organization of the “double tail” peptides appears to be closely related to electrostatically driven diffusional motions of the primary aggregates and nanofilaments. The diffusional freedom degrees are prompted by the formation of a dynamic ternary air/liquid/substrate interface, due to the water evaporation process from the ultrathin films of the peptide solution cast onto a solid mica substrate. Overall, the initial aggregation of unstructured round-shaped moieties, for both the peptides, can be seen as an entropy-driven process, involving the intra- and intermolecular interactions of hydrophobic parts of the peptides, while the further formation of long nanoribbons, only for “double tail” peptides, can be viewed in terms of an enthalpy-driven process, mainly due to the predominant electrostatic interactions between the charged heads of the interacting peptides. The role of the solid–liquid interface, as the locus of the enthalpy-driven linear organization, is also highlighted.
format Online
Article
Text
id pubmed-9418424
institution National Center for Biotechnology Information
language English
publishDate 2021
publisher RSC
record_format MEDLINE/PubMed
spelling pubmed-94184242022-09-20 From nanoaggregates to mesoscale ribbons: the multistep self-organization of amphiphilic peptides Messina, Grazia M. L. Mazzuca, Claudia Dettin, Monica Zamuner, Annj Di Napoli, Benedetta Ripani, Giorgio Marletta, Giovanni Palleschi, Antonio Nanoscale Adv Chemistry This paper reports atomic force microscopy results and molecular dynamics simulations of the striking differences of long-term self-organization structures of negatively charged (AcA(4))(2)KD (double tail) and AcA(4)D (single tail) peptides, respectively, forming micrometer-long, linearly ordered ribbon-like structures and nanometer-sized, unstructured, round-shaped aggregates. The subsequent formation steps of the long-range nanoribbons, experimentally observed only for the “double tail” (AcA(4))(2)KD peptide, are analyzed in detail, showing that the initial “primary” unstructured round-shaped aggregates progressively evolve into longer nanofilaments and into micrometer-long, network-forming nanoribbon moieties. In particular, the long-range self-organization of the “double tail” peptides appears to be closely related to electrostatically driven diffusional motions of the primary aggregates and nanofilaments. The diffusional freedom degrees are prompted by the formation of a dynamic ternary air/liquid/substrate interface, due to the water evaporation process from the ultrathin films of the peptide solution cast onto a solid mica substrate. Overall, the initial aggregation of unstructured round-shaped moieties, for both the peptides, can be seen as an entropy-driven process, involving the intra- and intermolecular interactions of hydrophobic parts of the peptides, while the further formation of long nanoribbons, only for “double tail” peptides, can be viewed in terms of an enthalpy-driven process, mainly due to the predominant electrostatic interactions between the charged heads of the interacting peptides. The role of the solid–liquid interface, as the locus of the enthalpy-driven linear organization, is also highlighted. RSC 2021-04-27 /pmc/articles/PMC9418424/ /pubmed/36133720 http://dx.doi.org/10.1039/d1na00216c Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by-nc/3.0/
spellingShingle Chemistry
Messina, Grazia M. L.
Mazzuca, Claudia
Dettin, Monica
Zamuner, Annj
Di Napoli, Benedetta
Ripani, Giorgio
Marletta, Giovanni
Palleschi, Antonio
From nanoaggregates to mesoscale ribbons: the multistep self-organization of amphiphilic peptides
title From nanoaggregates to mesoscale ribbons: the multistep self-organization of amphiphilic peptides
title_full From nanoaggregates to mesoscale ribbons: the multistep self-organization of amphiphilic peptides
title_fullStr From nanoaggregates to mesoscale ribbons: the multistep self-organization of amphiphilic peptides
title_full_unstemmed From nanoaggregates to mesoscale ribbons: the multistep self-organization of amphiphilic peptides
title_short From nanoaggregates to mesoscale ribbons: the multistep self-organization of amphiphilic peptides
title_sort from nanoaggregates to mesoscale ribbons: the multistep self-organization of amphiphilic peptides
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9418424/
https://www.ncbi.nlm.nih.gov/pubmed/36133720
http://dx.doi.org/10.1039/d1na00216c
work_keys_str_mv AT messinagraziaml fromnanoaggregatestomesoscaleribbonsthemultistepselforganizationofamphiphilicpeptides
AT mazzucaclaudia fromnanoaggregatestomesoscaleribbonsthemultistepselforganizationofamphiphilicpeptides
AT dettinmonica fromnanoaggregatestomesoscaleribbonsthemultistepselforganizationofamphiphilicpeptides
AT zamunerannj fromnanoaggregatestomesoscaleribbonsthemultistepselforganizationofamphiphilicpeptides
AT dinapolibenedetta fromnanoaggregatestomesoscaleribbonsthemultistepselforganizationofamphiphilicpeptides
AT ripanigiorgio fromnanoaggregatestomesoscaleribbonsthemultistepselforganizationofamphiphilicpeptides
AT marlettagiovanni fromnanoaggregatestomesoscaleribbonsthemultistepselforganizationofamphiphilicpeptides
AT palleschiantonio fromnanoaggregatestomesoscaleribbonsthemultistepselforganizationofamphiphilicpeptides