Novel noscapine derivatives stabilize the native state of insulin against fibrillation

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Standard

Novel noscapine derivatives stabilize the native state of insulin against fibrillation. / Alijanvand, Saeid Hadi; Christensen, Mikkel Hovden; Christiansen, Gunna; Harikandei, Kosar Babanezhad; Salehi, Peyman; Schiøtt, Birgit; Moosavi-Movahedi, Ali Akbar; Otzen, Daniel E.

I: International Journal of Biological Macromolecules, Bind 147, 03.2020, s. 98-108.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Alijanvand, SH, Christensen, MH, Christiansen, G, Harikandei, KB, Salehi, P, Schiøtt, B, Moosavi-Movahedi, AA & Otzen, DE 2020, 'Novel noscapine derivatives stabilize the native state of insulin against fibrillation', International Journal of Biological Macromolecules, bind 147, s. 98-108. https://doi.org/10.1016/j.ijbiomac.2020.01.061

APA

Alijanvand, S. H., Christensen, M. H., Christiansen, G., Harikandei, K. B., Salehi, P., Schiøtt, B., Moosavi-Movahedi, A. A., & Otzen, D. E. (2020). Novel noscapine derivatives stabilize the native state of insulin against fibrillation. International Journal of Biological Macromolecules, 147, 98-108. https://doi.org/10.1016/j.ijbiomac.2020.01.061

CBE

Alijanvand SH, Christensen MH, Christiansen G, Harikandei KB, Salehi P, Schiøtt B, Moosavi-Movahedi AA, Otzen DE. 2020. Novel noscapine derivatives stabilize the native state of insulin against fibrillation. International Journal of Biological Macromolecules. 147:98-108. https://doi.org/10.1016/j.ijbiomac.2020.01.061

MLA

Alijanvand, Saeid Hadi o.a.. "Novel noscapine derivatives stabilize the native state of insulin against fibrillation". International Journal of Biological Macromolecules. 2020, 147. 98-108. https://doi.org/10.1016/j.ijbiomac.2020.01.061

Vancouver

Alijanvand SH, Christensen MH, Christiansen G, Harikandei KB, Salehi P, Schiøtt B o.a. Novel noscapine derivatives stabilize the native state of insulin against fibrillation. International Journal of Biological Macromolecules. 2020 mar;147:98-108. https://doi.org/10.1016/j.ijbiomac.2020.01.061

Author

Alijanvand, Saeid Hadi ; Christensen, Mikkel Hovden ; Christiansen, Gunna ; Harikandei, Kosar Babanezhad ; Salehi, Peyman ; Schiøtt, Birgit ; Moosavi-Movahedi, Ali Akbar ; Otzen, Daniel E. / Novel noscapine derivatives stabilize the native state of insulin against fibrillation. I: International Journal of Biological Macromolecules. 2020 ; Bind 147. s. 98-108.

Bibtex

@article{b2663af08b4348f1aa0b73d81a0b10b0,
title = "Novel noscapine derivatives stabilize the native state of insulin against fibrillation",
abstract = "Protein aggregation to form amyloid is associated with many human diseases, increasing the need to develop inhibitors of this process. Here we evaluate the ability of derivatives of the small organic compound noscapine, derived from the opium poppy, to inhibit fibrillation of the model protein insulin. We combined biophysical methods to assess insulin stability and aggregation with computational docking and cell viability studies to identify the most potent derivatives. The best aggregation inhibitor (a phenyl derivative of N-nornoscapine) also demonstrated the highest ability to stabilize native insulin against thermal denaturation. This compound maintained insulin largely in the monomeric and natively folded state under fibrillation conditions and also decreased insulin aggregate toxicity against human neuroblastoma SH-SY5Y cells. The inhibitory effects were specific for insulin fibrillation, as the noscapine compounds did not inhibit fibrillation of other proteins such as α-synuclein, Aβ, and FapC. Our data demonstrate that compounds which stabilize the folded native state of a protein can not only inhibit fibrillation but also decrease the toxicity of the mature fibrillar aggregates of insulin protein.",
keywords = "Cell viability, Insulin, Noscapine, Protein fibrillation inhibitors, Protein ligands",
author = "Alijanvand, {Saeid Hadi} and Christensen, {Mikkel Hovden} and Gunna Christiansen and Harikandei, {Kosar Babanezhad} and Peyman Salehi and Birgit Schi{\o}tt and Moosavi-Movahedi, {Ali Akbar} and Otzen, {Daniel E}",
note = "Copyright {\textcopyright} 2020. Published by Elsevier B.V.",
year = "2020",
month = mar,
doi = "10.1016/j.ijbiomac.2020.01.061",
language = "English",
volume = "147",
pages = "98--108",
journal = "International Journal of Biological Macromolecules",
issn = "0141-8130",
publisher = "Elsevier BV",

}

RIS

TY - JOUR

T1 - Novel noscapine derivatives stabilize the native state of insulin against fibrillation

AU - Alijanvand, Saeid Hadi

AU - Christensen, Mikkel Hovden

AU - Christiansen, Gunna

AU - Harikandei, Kosar Babanezhad

AU - Salehi, Peyman

AU - Schiøtt, Birgit

AU - Moosavi-Movahedi, Ali Akbar

AU - Otzen, Daniel E

N1 - Copyright © 2020. Published by Elsevier B.V.

PY - 2020/3

Y1 - 2020/3

N2 - Protein aggregation to form amyloid is associated with many human diseases, increasing the need to develop inhibitors of this process. Here we evaluate the ability of derivatives of the small organic compound noscapine, derived from the opium poppy, to inhibit fibrillation of the model protein insulin. We combined biophysical methods to assess insulin stability and aggregation with computational docking and cell viability studies to identify the most potent derivatives. The best aggregation inhibitor (a phenyl derivative of N-nornoscapine) also demonstrated the highest ability to stabilize native insulin against thermal denaturation. This compound maintained insulin largely in the monomeric and natively folded state under fibrillation conditions and also decreased insulin aggregate toxicity against human neuroblastoma SH-SY5Y cells. The inhibitory effects were specific for insulin fibrillation, as the noscapine compounds did not inhibit fibrillation of other proteins such as α-synuclein, Aβ, and FapC. Our data demonstrate that compounds which stabilize the folded native state of a protein can not only inhibit fibrillation but also decrease the toxicity of the mature fibrillar aggregates of insulin protein.

AB - Protein aggregation to form amyloid is associated with many human diseases, increasing the need to develop inhibitors of this process. Here we evaluate the ability of derivatives of the small organic compound noscapine, derived from the opium poppy, to inhibit fibrillation of the model protein insulin. We combined biophysical methods to assess insulin stability and aggregation with computational docking and cell viability studies to identify the most potent derivatives. The best aggregation inhibitor (a phenyl derivative of N-nornoscapine) also demonstrated the highest ability to stabilize native insulin against thermal denaturation. This compound maintained insulin largely in the monomeric and natively folded state under fibrillation conditions and also decreased insulin aggregate toxicity against human neuroblastoma SH-SY5Y cells. The inhibitory effects were specific for insulin fibrillation, as the noscapine compounds did not inhibit fibrillation of other proteins such as α-synuclein, Aβ, and FapC. Our data demonstrate that compounds which stabilize the folded native state of a protein can not only inhibit fibrillation but also decrease the toxicity of the mature fibrillar aggregates of insulin protein.

KW - Cell viability

KW - Insulin

KW - Noscapine

KW - Protein fibrillation inhibitors

KW - Protein ligands

U2 - 10.1016/j.ijbiomac.2020.01.061

DO - 10.1016/j.ijbiomac.2020.01.061

M3 - Journal article

C2 - 31923504

VL - 147

SP - 98

EP - 108

JO - International Journal of Biological Macromolecules

JF - International Journal of Biological Macromolecules

SN - 0141-8130

ER -