Identifying Biological and Biophysical Features of Different Maturation States of α-Synuclein Amyloid Fibrils

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Identifying Biological and Biophysical Features of Different Maturation States of α-Synuclein Amyloid Fibrils. / Skamris, Thomas; Vestergaard, Bente; Madsen, Kenneth L.; Langkilde, Annette E.; Foderà, Vito.

In: Methods in molecular biology (Clifton, N.J.), Vol. 2551, 2023, p. 321-344.

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

Harvard

Skamris, T, Vestergaard, B, Madsen, KL, Langkilde, AE & Foderà, V 2023, 'Identifying Biological and Biophysical Features of Different Maturation States of α-Synuclein Amyloid Fibrils', Methods in molecular biology (Clifton, N.J.), vol. 2551, pp. 321-344. https://doi.org/10.1007/978-1-0716-2597-2_22

APA

Skamris, T., Vestergaard, B., Madsen, K. L., Langkilde, A. E., & Foderà, V. (2023). Identifying Biological and Biophysical Features of Different Maturation States of α-Synuclein Amyloid Fibrils. Methods in molecular biology (Clifton, N.J.), 2551, 321-344. https://doi.org/10.1007/978-1-0716-2597-2_22

Vancouver

Skamris T, Vestergaard B, Madsen KL, Langkilde AE, Foderà V. Identifying Biological and Biophysical Features of Different Maturation States of α-Synuclein Amyloid Fibrils. Methods in molecular biology (Clifton, N.J.). 2023;2551:321-344. https://doi.org/10.1007/978-1-0716-2597-2_22

Author

Skamris, Thomas ; Vestergaard, Bente ; Madsen, Kenneth L. ; Langkilde, Annette E. ; Foderà, Vito. / Identifying Biological and Biophysical Features of Different Maturation States of α-Synuclein Amyloid Fibrils. In: Methods in molecular biology (Clifton, N.J.). 2023 ; Vol. 2551. pp. 321-344.

Bibtex

@article{d462920f75454b9ea843a79409e1525f,

title = "Identifying Biological and Biophysical Features of Different Maturation States of α-Synuclein Amyloid Fibrils",

abstract = "Protein aggregates, hereunder amyloid fibrils, can undergo a maturation process, whereby early formed aggregates undergo a structural and physicochemical transition leading to more mature species. In the case of amyloid-related diseases, such maturation confers distinctive biological properties of the aggregates, which may account for a range of diverse pathological subtypes. Here, we present a protocol for the preparation of α-synuclein amyloid fibrils differing in the level of their maturation. We utilize widely accessible biophysical techniques to characterize the structure and morphology and a simple thermal treatment procedure to test their thermodynamic stability. Their biological properties are probed by means of binding to native plasma membrane sheets originating from mammalian cell lines.",

keywords = "Amyloid fibril maturation, Amyloid polymorphism, Fibril stability, Membrane binding, α-synuclein",

author = "Thomas Skamris and Bente Vestergaard and Madsen, {Kenneth L.} and Langkilde, {Annette E.} and Vito Foder{\`a}",

note = "Publisher Copyright: {\textcopyright} 2023. Springer Science+Business Media, LLC, part of Springer Nature.",

year = "2023",

doi = "10.1007/978-1-0716-2597-2_22",

language = "English",

volume = "2551",

pages = "321--344",

journal = "Methods in Molecular Biology",

issn = "1064-3745",

publisher = "Humana Press",

}

RIS

TY - JOUR

T1 - Identifying Biological and Biophysical Features of Different Maturation States of α-Synuclein Amyloid Fibrils

AU - Skamris, Thomas

AU - Vestergaard, Bente

AU - Madsen, Kenneth L.

AU - Langkilde, Annette E.

AU - Foderà, Vito

PY - 2023

Y1 - 2023

N2 - Protein aggregates, hereunder amyloid fibrils, can undergo a maturation process, whereby early formed aggregates undergo a structural and physicochemical transition leading to more mature species. In the case of amyloid-related diseases, such maturation confers distinctive biological properties of the aggregates, which may account for a range of diverse pathological subtypes. Here, we present a protocol for the preparation of α-synuclein amyloid fibrils differing in the level of their maturation. We utilize widely accessible biophysical techniques to characterize the structure and morphology and a simple thermal treatment procedure to test their thermodynamic stability. Their biological properties are probed by means of binding to native plasma membrane sheets originating from mammalian cell lines.

AB - Protein aggregates, hereunder amyloid fibrils, can undergo a maturation process, whereby early formed aggregates undergo a structural and physicochemical transition leading to more mature species. In the case of amyloid-related diseases, such maturation confers distinctive biological properties of the aggregates, which may account for a range of diverse pathological subtypes. Here, we present a protocol for the preparation of α-synuclein amyloid fibrils differing in the level of their maturation. We utilize widely accessible biophysical techniques to characterize the structure and morphology and a simple thermal treatment procedure to test their thermodynamic stability. Their biological properties are probed by means of binding to native plasma membrane sheets originating from mammalian cell lines.

KW - Amyloid fibril maturation

KW - Amyloid polymorphism

KW - Fibril stability

KW - Membrane binding

KW - α-synuclein

U2 - 10.1007/978-1-0716-2597-2_22

DO - 10.1007/978-1-0716-2597-2_22

M3 - Journal article

C2 - 36310213

AN - SCOPUS:85141004487

VL - 2551

SP - 321

EP - 344

JO - Methods in Molecular Biology

JF - Methods in Molecular Biology

SN - 1064-3745

ER -

ID: 324823266

Department of Neuroscience