Formation of covalent di-tyrosine dimers in recombinant α-synuclein

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Formation of covalent di-tyrosine dimers in recombinant α-synuclein. / van Maarschalkerweerd, A; Pedersen, MN; Peterson, H; Nilsson, M; Nguyen, TTT; Skamris, T; Rand, K; Vetri, V; Langkilde, AE; Vestergaard, B.

In: Intrinsically Disordered Proteins, Vol. 3, No. 1, 19.10.2015, p. 1-12.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

van Maarschalkerweerd, A, Pedersen, MN, Peterson, H, Nilsson, M, Nguyen, TTT, Skamris, T, Rand, K, Vetri, V, Langkilde, AE & Vestergaard, B 2015, 'Formation of covalent di-tyrosine dimers in recombinant α-synuclein', Intrinsically Disordered Proteins, vol. 3, no. 1, pp. 1-12. https://doi.org/10.1080/21690707.2015.1071302

APA

van Maarschalkerweerd, A., Pedersen, MN., Peterson, H., Nilsson, M., Nguyen, TTT., Skamris, T., Rand, K., Vetri, V., Langkilde, AE., & Vestergaard, B. (2015). Formation of covalent di-tyrosine dimers in recombinant α-synuclein. Intrinsically Disordered Proteins, 3(1), 1-12. https://doi.org/10.1080/21690707.2015.1071302

Vancouver

van Maarschalkerweerd A, Pedersen MN, Peterson H, Nilsson M, Nguyen TTT, Skamris T et al. Formation of covalent di-tyrosine dimers in recombinant α-synuclein. Intrinsically Disordered Proteins. 2015 Oct 19;3(1):1-12. https://doi.org/10.1080/21690707.2015.1071302

Author

van Maarschalkerweerd, A ; Pedersen, MN ; Peterson, H ; Nilsson, M ; Nguyen, TTT ; Skamris, T ; Rand, K ; Vetri, V ; Langkilde, AE ; Vestergaard, B. / Formation of covalent di-tyrosine dimers in recombinant α-synuclein. In: Intrinsically Disordered Proteins. 2015 ; Vol. 3, No. 1. pp. 1-12.

Bibtex

@article{4c98f1ff97a44b559a99cd2fd53210e2,
title = "Formation of covalent di-tyrosine dimers in recombinant α-synuclein",
abstract = "Parkinson's disease is associated with fibril deposition in the diseased brain. Misfolding events of the intrinsically disordered synaptic protein α-synuclein are suggested to lead to the formation of transient oligomeric and cytotoxic species. The etiology of Parkinson's disease is further associated with mitochondrial dysfunction and formation of reactive oxygen species. Oxidative stress causes chemical modification of native α-synuclein, plausibly further influencing misfolding events. Here, we present evidence for the spontaneous formation of covalent di-tyrosine α-synuclein dimers in standard recombinant protein preparations, induced without extrinsic oxidative or nitrative agents. The dimers exhibit no secondary structure but advanced SAXS studies reveal an increased structural definition, resulting in a more hydrophobic micro-environment than the highly disordered monomer. Accordingly, monomers and dimers follow distinct fibrillation pathways.",
author = "{van Maarschalkerweerd}, A and MN Pedersen and H Peterson and M Nilsson and TTT Nguyen and T Skamris and K Rand and V Vetri and AE Langkilde and B Vestergaard",
note = "doi: 10.1080/21690707.2015.1071302",
year = "2015",
month = oct,
day = "19",
doi = "10.1080/21690707.2015.1071302",
language = "English",
volume = "3",
pages = "1--12",
journal = "Intrinsically Disordered Proteins",
issn = "null",
number = "1",

}

RIS

TY - JOUR

T1 - Formation of covalent di-tyrosine dimers in recombinant α-synuclein

AU - van Maarschalkerweerd, A

AU - Pedersen, MN

AU - Peterson, H

AU - Nilsson, M

AU - Nguyen, TTT

AU - Skamris, T

AU - Rand, K

AU - Vetri, V

AU - Langkilde, AE

AU - Vestergaard, B

N1 - doi: 10.1080/21690707.2015.1071302

PY - 2015/10/19

Y1 - 2015/10/19

N2 - Parkinson's disease is associated with fibril deposition in the diseased brain. Misfolding events of the intrinsically disordered synaptic protein α-synuclein are suggested to lead to the formation of transient oligomeric and cytotoxic species. The etiology of Parkinson's disease is further associated with mitochondrial dysfunction and formation of reactive oxygen species. Oxidative stress causes chemical modification of native α-synuclein, plausibly further influencing misfolding events. Here, we present evidence for the spontaneous formation of covalent di-tyrosine α-synuclein dimers in standard recombinant protein preparations, induced without extrinsic oxidative or nitrative agents. The dimers exhibit no secondary structure but advanced SAXS studies reveal an increased structural definition, resulting in a more hydrophobic micro-environment than the highly disordered monomer. Accordingly, monomers and dimers follow distinct fibrillation pathways.

AB - Parkinson's disease is associated with fibril deposition in the diseased brain. Misfolding events of the intrinsically disordered synaptic protein α-synuclein are suggested to lead to the formation of transient oligomeric and cytotoxic species. The etiology of Parkinson's disease is further associated with mitochondrial dysfunction and formation of reactive oxygen species. Oxidative stress causes chemical modification of native α-synuclein, plausibly further influencing misfolding events. Here, we present evidence for the spontaneous formation of covalent di-tyrosine α-synuclein dimers in standard recombinant protein preparations, induced without extrinsic oxidative or nitrative agents. The dimers exhibit no secondary structure but advanced SAXS studies reveal an increased structural definition, resulting in a more hydrophobic micro-environment than the highly disordered monomer. Accordingly, monomers and dimers follow distinct fibrillation pathways.

U2 - 10.1080/21690707.2015.1071302

DO - 10.1080/21690707.2015.1071302

M3 - Journal article

VL - 3

SP - 1

EP - 12

JO - Intrinsically Disordered Proteins

JF - Intrinsically Disordered Proteins

SN - null

IS - 1

ER -

ID: 148551955