Rapid fragmentation during seeded lysozyme aggregation revealed at the single molecule level

Research output: Contribution to journalArticle

Standard

Rapid fragmentation during seeded lysozyme aggregation revealed at the single molecule level. / Kubankova, Marketa; Lin, Xiaoyan; Albrecht, Tim; Edel, Joshua B; Kuimova, Marina K.

In: Analytical Chemistry, Vol. 91, No. 10, 21.05.2019, p. 6880-6886.

Research output: Contribution to journalArticle

Harvard

APA

Vancouver

Author

Kubankova, Marketa ; Lin, Xiaoyan ; Albrecht, Tim ; Edel, Joshua B ; Kuimova, Marina K. / Rapid fragmentation during seeded lysozyme aggregation revealed at the single molecule level. In: Analytical Chemistry. 2019 ; Vol. 91, No. 10. pp. 6880-6886.

Bibtex

@article{872e0cb2f26b41bfb23ea542abc60eb9,
title = "Rapid fragmentation during seeded lysozyme aggregation revealed at the single molecule level",
abstract = "Protein aggregation is associated with neurodegenerative disorders such as Alzheimer's and Parkinson's diseases. The poorly understood pathogenic mechanism of amyloid diseases makes early stage diagnostics or therapeutic intervention a challenge. Seeded polymerization that reduces the duration of the lag phase and accelerates fibril growth is a widespread model to study amyloid formation. Seeding effects are hypothesized to be important in the {"}infectivity{"} of amyloids and are linked to the development of systemic amyloidosis in vivo. The exact mechanism of seeding is unclear yet critical to illuminating the propagation of amyloids. Here we report on the lateral and axial fragmentation of seed fibrils in the presence of lysozyme monomers at short time scales, followed by the generation of oligomers and growth of fibrils.",
author = "Marketa Kubankova and Xiaoyan Lin and Tim Albrecht and Edel, {Joshua B} and Kuimova, {Marina K}",
year = "2019",
month = may,
day = "21",
doi = "10.1021/acs.analchem.9b01221",
language = "English",
volume = "91",
pages = "6880--6886",
journal = "Analytical Chemistry",
issn = "0003-2700",
publisher = "American Chemical Society",
number = "10",

}

RIS

TY - JOUR

T1 - Rapid fragmentation during seeded lysozyme aggregation revealed at the single molecule level

AU - Kubankova, Marketa

AU - Lin, Xiaoyan

AU - Albrecht, Tim

AU - Edel, Joshua B

AU - Kuimova, Marina K

PY - 2019/5/21

Y1 - 2019/5/21

N2 - Protein aggregation is associated with neurodegenerative disorders such as Alzheimer's and Parkinson's diseases. The poorly understood pathogenic mechanism of amyloid diseases makes early stage diagnostics or therapeutic intervention a challenge. Seeded polymerization that reduces the duration of the lag phase and accelerates fibril growth is a widespread model to study amyloid formation. Seeding effects are hypothesized to be important in the "infectivity" of amyloids and are linked to the development of systemic amyloidosis in vivo. The exact mechanism of seeding is unclear yet critical to illuminating the propagation of amyloids. Here we report on the lateral and axial fragmentation of seed fibrils in the presence of lysozyme monomers at short time scales, followed by the generation of oligomers and growth of fibrils.

AB - Protein aggregation is associated with neurodegenerative disorders such as Alzheimer's and Parkinson's diseases. The poorly understood pathogenic mechanism of amyloid diseases makes early stage diagnostics or therapeutic intervention a challenge. Seeded polymerization that reduces the duration of the lag phase and accelerates fibril growth is a widespread model to study amyloid formation. Seeding effects are hypothesized to be important in the "infectivity" of amyloids and are linked to the development of systemic amyloidosis in vivo. The exact mechanism of seeding is unclear yet critical to illuminating the propagation of amyloids. Here we report on the lateral and axial fragmentation of seed fibrils in the presence of lysozyme monomers at short time scales, followed by the generation of oligomers and growth of fibrils.

UR - http://www.scopus.com/inward/record.url?scp=85065874510&partnerID=8YFLogxK

U2 - 10.1021/acs.analchem.9b01221

DO - 10.1021/acs.analchem.9b01221

M3 - Article

C2 - 30999745

VL - 91

SP - 6880

EP - 6886

JO - Analytical Chemistry

JF - Analytical Chemistry

SN - 0003-2700

IS - 10

ER -