Beta sheets with a twist: The conformation of helical polyisocyanopeptides determined by using vibrational circular dichroism

E. Schwartz, V. Liégeois, M. Koepf, P. Bodis, J.J.L.M. Cornelissen, P. Brocorens, D. Beljonne, R.J.M. Nolte, A.E. Rowan, S. Woutersen, B. Champagne

Résultats de recherche: Contribution à un journal/une revueArticle

Résumé

Detailed information on the architecture of polyisocyanopeptides based on vibrational circular dichroism (VCD) spectroscopy in combination with DFT calculations is presented. It is demonstrated that the screw sense of the helical polyisocyanides can be determined directly from the Cï£N- stretch vibrational region of the VCD spectrum. Analysis of the VCD signals associated with the amideI and amideII modes provides detailed information on the peptide side-chain arrangement in the polymer and indicates the presence of a helical β-sheet architecture, in which the dihedral angles are slightly different to those of natural β-sheet helices. Good vibrations: The structure elucidation of helical polyisocyanides derived from alanylalanine (PIAA; see figure) by using a combination of DFT calculations and vibrational circular dichroism (VCD) spectroscopy is described. An accurate description of the conformation of the PIAA is attained, which contributes to the current understanding of the conformational architecture of polyisocyanides.
langue originaleAnglais
Pages (de - à)13168-13174
Nombre de pages7
journalChemistry: A European Journal
Volume19
Numéro de publication39
Les DOIs
étatPublié - 23 sept. 2013

Empreinte digitale

Conformations
Circular dichroism spectroscopy
Vibrational spectroscopy
Discrete Fourier transforms
Dihedral angle
Peptides
Polymers
Circular Dichroism

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Schwartz, E. ; Liégeois, V. ; Koepf, M. ; Bodis, P. ; Cornelissen, J.J.L.M. ; Brocorens, P. ; Beljonne, D. ; Nolte, R.J.M. ; Rowan, A.E. ; Woutersen, S. ; Champagne, B. / Beta sheets with a twist : The conformation of helical polyisocyanopeptides determined by using vibrational circular dichroism. Dans: Chemistry: A European Journal. 2013 ; Vol 19, Numéro 39. p. 13168-13174.
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abstract = "Detailed information on the architecture of polyisocyanopeptides based on vibrational circular dichroism (VCD) spectroscopy in combination with DFT calculations is presented. It is demonstrated that the screw sense of the helical polyisocyanides can be determined directly from the C{\"i}£N- stretch vibrational region of the VCD spectrum. Analysis of the VCD signals associated with the amideI and amideII modes provides detailed information on the peptide side-chain arrangement in the polymer and indicates the presence of a helical β-sheet architecture, in which the dihedral angles are slightly different to those of natural β-sheet helices. Good vibrations: The structure elucidation of helical polyisocyanides derived from alanylalanine (PIAA; see figure) by using a combination of DFT calculations and vibrational circular dichroism (VCD) spectroscopy is described. An accurate description of the conformation of the PIAA is attained, which contributes to the current understanding of the conformational architecture of polyisocyanides.",
author = "E. Schwartz and V. Li{\'e}geois and M. Koepf and P. Bodis and J.J.L.M. Cornelissen and P. Brocorens and D. Beljonne and R.J.M. Nolte and A.E. Rowan and S. Woutersen and B. Champagne",
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Schwartz, E, Liégeois, V, Koepf, M, Bodis, P, Cornelissen, JJLM, Brocorens, P, Beljonne, D, Nolte, RJM, Rowan, AE, Woutersen, S & Champagne, B 2013, 'Beta sheets with a twist: The conformation of helical polyisocyanopeptides determined by using vibrational circular dichroism', Chemistry: A European Journal, VOL. 19, Numéro 39, p. 13168-13174. https://doi.org/10.1002/chem.201300073

Beta sheets with a twist : The conformation of helical polyisocyanopeptides determined by using vibrational circular dichroism. / Schwartz, E.; Liégeois, V.; Koepf, M.; Bodis, P.; Cornelissen, J.J.L.M.; Brocorens, P.; Beljonne, D.; Nolte, R.J.M.; Rowan, A.E.; Woutersen, S.; Champagne, B.

Dans: Chemistry: A European Journal, Vol 19, Numéro 39, 23.09.2013, p. 13168-13174.

Résultats de recherche: Contribution à un journal/une revueArticle

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T2 - The conformation of helical polyisocyanopeptides determined by using vibrational circular dichroism

AU - Schwartz, E.

AU - Liégeois, V.

AU - Koepf, M.

AU - Bodis, P.

AU - Cornelissen, J.J.L.M.

AU - Brocorens, P.

AU - Beljonne, D.

AU - Nolte, R.J.M.

AU - Rowan, A.E.

AU - Woutersen, S.

AU - Champagne, B.

PY - 2013/9/23

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N2 - Detailed information on the architecture of polyisocyanopeptides based on vibrational circular dichroism (VCD) spectroscopy in combination with DFT calculations is presented. It is demonstrated that the screw sense of the helical polyisocyanides can be determined directly from the Cï£N- stretch vibrational region of the VCD spectrum. Analysis of the VCD signals associated with the amideI and amideII modes provides detailed information on the peptide side-chain arrangement in the polymer and indicates the presence of a helical β-sheet architecture, in which the dihedral angles are slightly different to those of natural β-sheet helices. Good vibrations: The structure elucidation of helical polyisocyanides derived from alanylalanine (PIAA; see figure) by using a combination of DFT calculations and vibrational circular dichroism (VCD) spectroscopy is described. An accurate description of the conformation of the PIAA is attained, which contributes to the current understanding of the conformational architecture of polyisocyanides.

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