Amyloidogenicity as a driving force for the formation of functional oligomers

Standard

Amyloidogenicity as a driving force for the formation of functional oligomers. / Azizyan, Rafayel A.; Wang, Weiqiang; Anikeenko, Alexey et al.

In: Journal of Structural Biology, Vol. 212, No. 1, 107604, 01.10.2020.

Research output: Contribution to journal › Article › peer-review

Harvard

Azizyan, RA, Wang, W, Anikeenko, A, Radkova, Z, Bakulina, A, Garro, A, Charlier, L, Dumas, C, Ventura, S & Kajava, AV 2020, 'Amyloidogenicity as a driving force for the formation of functional oligomers', Journal of Structural Biology, vol. 212, no. 1, 107604. https://doi.org/10.1016/j.jsb.2020.107604

APA

Azizyan, R. A., Wang, W., Anikeenko, A., Radkova, Z., Bakulina, A., Garro, A., Charlier, L., Dumas, C., Ventura, S., & Kajava, A. V. (2020). Amyloidogenicity as a driving force for the formation of functional oligomers. Journal of Structural Biology, 212(1), [107604]. https://doi.org/10.1016/j.jsb.2020.107604

Vancouver

Azizyan RA, Wang W, Anikeenko A, Radkova Z, Bakulina A, Garro A et al. Amyloidogenicity as a driving force for the formation of functional oligomers. Journal of Structural Biology. 2020 Oct 1;212(1):107604. doi: 10.1016/j.jsb.2020.107604

Author

Azizyan, Rafayel A. ; Wang, Weiqiang ; Anikeenko, Alexey et al. / Amyloidogenicity as a driving force for the formation of functional oligomers. In: Journal of Structural Biology. 2020 ; Vol. 212, No. 1.

BibTeX

@article{be34efe550bc4e67a21bdc9e17d4f1b4,

title = "Amyloidogenicity as a driving force for the formation of functional oligomers",

abstract = "Insoluble amyloid fibrils formed by self-assembly of amyloidogenic regions of proteins have a cross-β-structure. In this work, by using targeted molecular dynamics and rigid body simulation, we demonstrate that if a protein consists of an amyloidogenic region and a globular domain(s) and if the linker between them is short enough, such molecules cannot assemble into amyloid fibrils, instead, they form oligomers with a defined and limited number of β-strands in the cross-β core. We show that this blockage of the amyloid growth is due to the steric repulsion of the globular structures linked to amyloidogenic regions. Furthermore, we establish a relationship between the linker length and the number of monomers in such nanoparticles. We hypothesise that such oligomerisation can be a yet unrecognised way to form natural protein complexes involved in biological processes. Our results can also be used in protein engineering for designing soluble nanoparticles carrying different functional domains.",

keywords = "Amyloids, Functional nanoparticles, Rigid body simulation, Targeted molecular dynamics, PHASE-SEPARATION, PRION DOMAIN, AMYLOID FIBRILS, MODELS, SUP35P, PARALLEL BETA-SHEET, ALPHA-SYNUCLEIN, AGGREGATION",

author = "Azizyan, {Rafayel A.} and Weiqiang Wang and Alexey Anikeenko and Zinaida Radkova and Anastasia Bakulina and Adriana Garro and Landry Charlier and Christian Dumas and Salvador Ventura and Kajava, {Andrey V.}",

year = "2020",

month = oct,

day = "1",

doi = "10.1016/j.jsb.2020.107604",

language = "English",

volume = "212",

journal = "Journal of Structural Biology",

issn = "1047-8477",

publisher = "Elsevier",

number = "1",

}

RIS

TY - JOUR

T1 - Amyloidogenicity as a driving force for the formation of functional oligomers

AU - Azizyan, Rafayel A.

AU - Wang, Weiqiang

AU - Anikeenko, Alexey

AU - Radkova, Zinaida

AU - Bakulina, Anastasia

AU - Garro, Adriana

AU - Charlier, Landry

AU - Dumas, Christian

AU - Ventura, Salvador

AU - Kajava, Andrey V.

PY - 2020/10/1

Y1 - 2020/10/1

N2 - Insoluble amyloid fibrils formed by self-assembly of amyloidogenic regions of proteins have a cross-β-structure. In this work, by using targeted molecular dynamics and rigid body simulation, we demonstrate that if a protein consists of an amyloidogenic region and a globular domain(s) and if the linker between them is short enough, such molecules cannot assemble into amyloid fibrils, instead, they form oligomers with a defined and limited number of β-strands in the cross-β core. We show that this blockage of the amyloid growth is due to the steric repulsion of the globular structures linked to amyloidogenic regions. Furthermore, we establish a relationship between the linker length and the number of monomers in such nanoparticles. We hypothesise that such oligomerisation can be a yet unrecognised way to form natural protein complexes involved in biological processes. Our results can also be used in protein engineering for designing soluble nanoparticles carrying different functional domains.

AB - Insoluble amyloid fibrils formed by self-assembly of amyloidogenic regions of proteins have a cross-β-structure. In this work, by using targeted molecular dynamics and rigid body simulation, we demonstrate that if a protein consists of an amyloidogenic region and a globular domain(s) and if the linker between them is short enough, such molecules cannot assemble into amyloid fibrils, instead, they form oligomers with a defined and limited number of β-strands in the cross-β core. We show that this blockage of the amyloid growth is due to the steric repulsion of the globular structures linked to amyloidogenic regions. Furthermore, we establish a relationship between the linker length and the number of monomers in such nanoparticles. We hypothesise that such oligomerisation can be a yet unrecognised way to form natural protein complexes involved in biological processes. Our results can also be used in protein engineering for designing soluble nanoparticles carrying different functional domains.

KW - Amyloids

KW - Functional nanoparticles

KW - Rigid body simulation

KW - Targeted molecular dynamics

KW - PHASE-SEPARATION

KW - PRION DOMAIN

KW - AMYLOID FIBRILS

KW - MODELS

KW - SUP35P

KW - PARALLEL BETA-SHEET

KW - ALPHA-SYNUCLEIN

KW - AGGREGATION

UR - http://www.scopus.com/inward/record.url?scp=85089518419&partnerID=8YFLogxK

U2 - 10.1016/j.jsb.2020.107604

DO - 10.1016/j.jsb.2020.107604

M3 - Article

C2 - 32805411

AN - SCOPUS:85089518419

VL - 212

JO - Journal of Structural Biology

JF - Journal of Structural Biology

SN - 1047-8477

IS - 1

M1 - 107604

ER -

ID: 25298923