Structural and spectroscopic properties of assemblies of self-replicating peptide macrocycles

Pim W.J.M. Frederix, Julien Ide, Y. Altay, Gael Schaeffer, Mathieu Surin, David Beljonne, Anna S. Bondarenko, Thomas L.C. Jansen, Sijbren Otto, Siewert J. Marrink

Research output: Contribution to journalArticleAcademicpeer-review

9 Citations (Scopus)
2 Downloads (Pure)

Abstract

Self-replication at the molecular level is often seen as essential to the early origins of life. Recently a mechanism of self-replication has been discovered in which replicator self-assembly drives the process. We have studied one of the examples of such self-assembling self-replicating molecules to a high level of structural detail using a combination of computational and spectroscopic techniques. Molecular Dynamics simulations of self-assembled stacks of peptide-derived replicators provide insights into the structural characteristics of the system and serve as the basis for semiempirical calculations of the UV–vis, circular dichroism (CD) and infrared (IR) absorption spectra that reflect the chiral organization and peptide secondary structure of the stacks. Two proposed structural models are tested by comparing calculated spectra to experimental data from electron microscopy, CD and IR spectroscopy, resulting in a better insight into the specific supramolecular interactions that lead to self-replication. Specifically, we find a cooperative self-assembly process in which β-sheet formation leads to well-organized structures, while also the aromatic core of the macrocycles plays an important role in the stability of the resulting fibers.
Original languageEnglish
Pages (from-to)7858-7868
Number of pages11
JournalACS Nano
Volume11
Issue number8
DOIs
Publication statusPublished - 2017
Externally publishedYes

Fingerprint

Self assembly
assemblies
Peptides
dichroism
peptides
self assembly
Circular dichroism spectroscopy
Infrared absorption
Dichroism
assembling
Electron microscopy
infrared absorption
Molecular dynamics
Absorption spectra
Infrared spectroscopy
electron microscopy
infrared spectra
infrared spectroscopy
molecular dynamics
absorption spectra

Cite this

Frederix, P. W. J. M., Ide, J., Altay, Y., Schaeffer, G., Surin, M., Beljonne, D., ... Marrink, S. J. (2017). Structural and spectroscopic properties of assemblies of self-replicating peptide macrocycles. ACS Nano, 11(8), 7858-7868. https://doi.org/10.1021/acsnano.7b02211
Frederix, Pim W.J.M. ; Ide, Julien ; Altay, Y. ; Schaeffer, Gael ; Surin, Mathieu ; Beljonne, David ; Bondarenko, Anna S. ; Jansen, Thomas L.C. ; Otto, Sijbren ; Marrink, Siewert J. / Structural and spectroscopic properties of assemblies of self-replicating peptide macrocycles. In: ACS Nano. 2017 ; Vol. 11, No. 8. pp. 7858-7868.
@article{436b638294da4966a98453003aed12c8,
title = "Structural and spectroscopic properties of assemblies of self-replicating peptide macrocycles",
abstract = "Self-replication at the molecular level is often seen as essential to the early origins of life. Recently a mechanism of self-replication has been discovered in which replicator self-assembly drives the process. We have studied one of the examples of such self-assembling self-replicating molecules to a high level of structural detail using a combination of computational and spectroscopic techniques. Molecular Dynamics simulations of self-assembled stacks of peptide-derived replicators provide insights into the structural characteristics of the system and serve as the basis for semiempirical calculations of the UV–vis, circular dichroism (CD) and infrared (IR) absorption spectra that reflect the chiral organization and peptide secondary structure of the stacks. Two proposed structural models are tested by comparing calculated spectra to experimental data from electron microscopy, CD and IR spectroscopy, resulting in a better insight into the specific supramolecular interactions that lead to self-replication. Specifically, we find a cooperative self-assembly process in which β-sheet formation leads to well-organized structures, while also the aromatic core of the macrocycles plays an important role in the stability of the resulting fibers.",
author = "Frederix, {Pim W.J.M.} and Julien Ide and Y. Altay and Gael Schaeffer and Mathieu Surin and David Beljonne and Bondarenko, {Anna S.} and Jansen, {Thomas L.C.} and Sijbren Otto and Marrink, {Siewert J.}",
year = "2017",
doi = "10.1021/acsnano.7b02211",
language = "English",
volume = "11",
pages = "7858--7868",
journal = "ACS Nano",
issn = "1936-0851",
publisher = "American Chemical Society",
number = "8",

}

Frederix, PWJM, Ide, J, Altay, Y, Schaeffer, G, Surin, M, Beljonne, D, Bondarenko, AS, Jansen, TLC, Otto, S & Marrink, SJ 2017, 'Structural and spectroscopic properties of assemblies of self-replicating peptide macrocycles', ACS Nano, vol. 11, no. 8, pp. 7858-7868. https://doi.org/10.1021/acsnano.7b02211

Structural and spectroscopic properties of assemblies of self-replicating peptide macrocycles. / Frederix, Pim W.J.M. ; Ide, Julien; Altay, Y.; Schaeffer, Gael; Surin, Mathieu; Beljonne, David; Bondarenko, Anna S.; Jansen, Thomas L.C. ; Otto, Sijbren; Marrink, Siewert J.

In: ACS Nano, Vol. 11, No. 8, 2017, p. 7858-7868.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Structural and spectroscopic properties of assemblies of self-replicating peptide macrocycles

AU - Frederix, Pim W.J.M.

AU - Ide, Julien

AU - Altay, Y.

AU - Schaeffer, Gael

AU - Surin, Mathieu

AU - Beljonne, David

AU - Bondarenko, Anna S.

AU - Jansen, Thomas L.C.

AU - Otto, Sijbren

AU - Marrink, Siewert J.

PY - 2017

Y1 - 2017

N2 - Self-replication at the molecular level is often seen as essential to the early origins of life. Recently a mechanism of self-replication has been discovered in which replicator self-assembly drives the process. We have studied one of the examples of such self-assembling self-replicating molecules to a high level of structural detail using a combination of computational and spectroscopic techniques. Molecular Dynamics simulations of self-assembled stacks of peptide-derived replicators provide insights into the structural characteristics of the system and serve as the basis for semiempirical calculations of the UV–vis, circular dichroism (CD) and infrared (IR) absorption spectra that reflect the chiral organization and peptide secondary structure of the stacks. Two proposed structural models are tested by comparing calculated spectra to experimental data from electron microscopy, CD and IR spectroscopy, resulting in a better insight into the specific supramolecular interactions that lead to self-replication. Specifically, we find a cooperative self-assembly process in which β-sheet formation leads to well-organized structures, while also the aromatic core of the macrocycles plays an important role in the stability of the resulting fibers.

AB - Self-replication at the molecular level is often seen as essential to the early origins of life. Recently a mechanism of self-replication has been discovered in which replicator self-assembly drives the process. We have studied one of the examples of such self-assembling self-replicating molecules to a high level of structural detail using a combination of computational and spectroscopic techniques. Molecular Dynamics simulations of self-assembled stacks of peptide-derived replicators provide insights into the structural characteristics of the system and serve as the basis for semiempirical calculations of the UV–vis, circular dichroism (CD) and infrared (IR) absorption spectra that reflect the chiral organization and peptide secondary structure of the stacks. Two proposed structural models are tested by comparing calculated spectra to experimental data from electron microscopy, CD and IR spectroscopy, resulting in a better insight into the specific supramolecular interactions that lead to self-replication. Specifically, we find a cooperative self-assembly process in which β-sheet formation leads to well-organized structures, while also the aromatic core of the macrocycles plays an important role in the stability of the resulting fibers.

U2 - 10.1021/acsnano.7b02211

DO - 10.1021/acsnano.7b02211

M3 - Article

C2 - 28723067

VL - 11

SP - 7858

EP - 7868

JO - ACS Nano

JF - ACS Nano

SN - 1936-0851

IS - 8

ER -