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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...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
RSC
2021
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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 |
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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 |
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