Crystal Structure of the DFNKF Segment of Human Calcitonin Unveils Aromatic Interactions between Phenylalanines

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Crystal Structure of the DFNKF Segment of Human Calcitonin Unveils Aromatic Interactions between Phenylalanines. / Bertolani, Arianna; Pizzi, Andrea; Pirrie, Lisa; Gazzera, Lara; Morra, Giulia; Meli, Massimiliano; Colombo, Giorgio; Genoni, Alessandro; Cavallo, Gabriella; Terraneo, Giancarlo; Metrangolo, Pierangelo.

In: CHEMISTRY: A EUROPEAN JOURNAL, Vol. 23, No. 9, 10.02.2017, p. 2051-2058.

Research output: Contribution to journalArticle

Harvard

Bertolani, A, Pizzi, A, Pirrie, L, Gazzera, L, Morra, G, Meli, M, Colombo, G, Genoni, A, Cavallo, G, Terraneo, G & Metrangolo, P 2017, 'Crystal Structure of the DFNKF Segment of Human Calcitonin Unveils Aromatic Interactions between Phenylalanines', CHEMISTRY: A EUROPEAN JOURNAL, vol. 23, no. 9, pp. 2051-2058. https://doi.org/10.1002/chem.201604639

APA

Bertolani, A., Pizzi, A., Pirrie, L., Gazzera, L., Morra, G., Meli, M., ... Metrangolo, P. (2017). Crystal Structure of the DFNKF Segment of Human Calcitonin Unveils Aromatic Interactions between Phenylalanines. CHEMISTRY: A EUROPEAN JOURNAL, 23(9), 2051-2058. https://doi.org/10.1002/chem.201604639

Vancouver

Author

Bertolani, Arianna ; Pizzi, Andrea ; Pirrie, Lisa ; Gazzera, Lara ; Morra, Giulia ; Meli, Massimiliano ; Colombo, Giorgio ; Genoni, Alessandro ; Cavallo, Gabriella ; Terraneo, Giancarlo ; Metrangolo, Pierangelo. / Crystal Structure of the DFNKF Segment of Human Calcitonin Unveils Aromatic Interactions between Phenylalanines. In: CHEMISTRY: A EUROPEAN JOURNAL. 2017 ; Vol. 23, No. 9. pp. 2051-2058.

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@article{19a382e8ccf14863af5f3ffd4ded028c,
title = "Crystal Structure of the DFNKF Segment of Human Calcitonin Unveils Aromatic Interactions between Phenylalanines",
abstract = "Although intensively studied, the high-resolution crystal structure of the peptide DFNKF, the core-segment of human calcitonin, has never been described. Here we report how the use of iodination as a strategy to promote crystallisation and facilitate phase determination, allowed us to solve, for the first time, the single-crystal X-ray structure of a DFNKF derivative. Computational studies suggest that both the iodinated and the wild-type peptides populate very similar conformations. Furthermore, the conformer found in the solid-state structure is one of the most populated in solution, making the crystal structure a reliable model for the peptide in solution. The crystal structure of DFNKF(I) confirms the overall features of the amyloid cross-β spine and highlights how aromatic-aromatic interactions are important structural factors in the self-assembly of this peptide. A detailed analysis of such interactions is reported.",
keywords = "Amyloid beta-peptides, Aromatic interactions, Crystal structures, Iodination, Peptides",
author = "Arianna Bertolani and Andrea Pizzi and Lisa Pirrie and Lara Gazzera and Giulia Morra and Massimiliano Meli and Giorgio Colombo and Alessandro Genoni and Gabriella Cavallo and Giancarlo Terraneo and Pierangelo Metrangolo",
year = "2017",
month = "2",
day = "10",
doi = "10.1002/chem.201604639",
language = "English",
volume = "23",
pages = "2051--2058",
journal = "CHEMISTRY: A EUROPEAN JOURNAL",
issn = "0947-6539",
number = "9",

}

RIS - Download

TY - JOUR

T1 - Crystal Structure of the DFNKF Segment of Human Calcitonin Unveils Aromatic Interactions between Phenylalanines

AU - Bertolani, Arianna

AU - Pizzi, Andrea

AU - Pirrie, Lisa

AU - Gazzera, Lara

AU - Morra, Giulia

AU - Meli, Massimiliano

AU - Colombo, Giorgio

AU - Genoni, Alessandro

AU - Cavallo, Gabriella

AU - Terraneo, Giancarlo

AU - Metrangolo, Pierangelo

PY - 2017/2/10

Y1 - 2017/2/10

N2 - Although intensively studied, the high-resolution crystal structure of the peptide DFNKF, the core-segment of human calcitonin, has never been described. Here we report how the use of iodination as a strategy to promote crystallisation and facilitate phase determination, allowed us to solve, for the first time, the single-crystal X-ray structure of a DFNKF derivative. Computational studies suggest that both the iodinated and the wild-type peptides populate very similar conformations. Furthermore, the conformer found in the solid-state structure is one of the most populated in solution, making the crystal structure a reliable model for the peptide in solution. The crystal structure of DFNKF(I) confirms the overall features of the amyloid cross-β spine and highlights how aromatic-aromatic interactions are important structural factors in the self-assembly of this peptide. A detailed analysis of such interactions is reported.

AB - Although intensively studied, the high-resolution crystal structure of the peptide DFNKF, the core-segment of human calcitonin, has never been described. Here we report how the use of iodination as a strategy to promote crystallisation and facilitate phase determination, allowed us to solve, for the first time, the single-crystal X-ray structure of a DFNKF derivative. Computational studies suggest that both the iodinated and the wild-type peptides populate very similar conformations. Furthermore, the conformer found in the solid-state structure is one of the most populated in solution, making the crystal structure a reliable model for the peptide in solution. The crystal structure of DFNKF(I) confirms the overall features of the amyloid cross-β spine and highlights how aromatic-aromatic interactions are important structural factors in the self-assembly of this peptide. A detailed analysis of such interactions is reported.

KW - Amyloid beta-peptides

KW - Aromatic interactions

KW - Crystal structures

KW - Iodination

KW - Peptides

UR - http://www.scopus.com/inward/record.url?scp=85007197255&partnerID=8YFLogxK

U2 - 10.1002/chem.201604639

DO - 10.1002/chem.201604639

M3 - Article

VL - 23

SP - 2051

EP - 2058

JO - CHEMISTRY: A EUROPEAN JOURNAL

JF - CHEMISTRY: A EUROPEAN JOURNAL

SN - 0947-6539

IS - 9

ER -

ID: 10383332