MODELIZATION OF AMYLOID FIBRIL SELF-ASSEMBLY
Intermolecular noncovalent interactions between protein molecules result in the formation of a wide spectrum of supramolecular assemblies the structure of which varies from disordered amorphous aggregates to the crystals with strictly defined translational symmetry in three directions. One-dimension...
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V.N. Karazin Kharkiv National University Publishing
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doaj-a414415c7f8d4a66aaf8da580b66ad092020-11-24T23:57:18ZengV.N. Karazin Kharkiv National University PublishingEast European Journal of Physics2312-43342312-45392018-04-0151475410239MODELIZATION OF AMYLOID FIBRIL SELF-ASSEMBLYV. Trusova0G. Gorbenko1Department of Nuclear and Medical Physics, V.N. Karazin Kharkiv National University 4 Svobody Sq., Kharkiv, 61022, UkraineDepartment of Nuclear and Medical Physics, V.N. Karazin Kharkiv National University 4 Svobody Sq., Kharkiv, 61022, UkraineIntermolecular noncovalent interactions between protein molecules result in the formation of a wide spectrum of supramolecular assemblies the structure of which varies from disordered amorphous aggregates to the crystals with strictly defined translational symmetry in three directions. One-dimensional protein aggregates (amyloid fibrils) represent highly ordered semiflexible polymers with unique mesoscopic properties which can be tuned by both intrinsic physicochemical characteristics of polypeptide chain and milieu conditions. In the present work the molecular mechanisms of amyloid formation are discussed and mathematical description of the existing models of protein fibrillization are given. For disease-related amyloids, deeper understanding of fibril growth process may shed light on the pathogenesis and molecular mechanisms of the disorders, as well as on the strategies of amyloidosis prevention at atomistic level. In the context of nanotechnology and functional material science, knowing the details of amyloid formation is crucially required for the design of novel nanomaterials with unprecedented qualities.http://periodicals.karazin.ua/eejp/article/view/10463amyloid fibrilsmisfoldingmathematical modelsamyloid diseasesnanomaterials |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
V. Trusova G. Gorbenko |
spellingShingle |
V. Trusova G. Gorbenko MODELIZATION OF AMYLOID FIBRIL SELF-ASSEMBLY East European Journal of Physics amyloid fibrils misfolding mathematical models amyloid diseases nanomaterials |
author_facet |
V. Trusova G. Gorbenko |
author_sort |
V. Trusova |
title |
MODELIZATION OF AMYLOID FIBRIL SELF-ASSEMBLY |
title_short |
MODELIZATION OF AMYLOID FIBRIL SELF-ASSEMBLY |
title_full |
MODELIZATION OF AMYLOID FIBRIL SELF-ASSEMBLY |
title_fullStr |
MODELIZATION OF AMYLOID FIBRIL SELF-ASSEMBLY |
title_full_unstemmed |
MODELIZATION OF AMYLOID FIBRIL SELF-ASSEMBLY |
title_sort |
modelization of amyloid fibril self-assembly |
publisher |
V.N. Karazin Kharkiv National University Publishing |
series |
East European Journal of Physics |
issn |
2312-4334 2312-4539 |
publishDate |
2018-04-01 |
description |
Intermolecular noncovalent interactions between protein molecules result in the formation of a wide spectrum of supramolecular assemblies the structure of which varies from disordered amorphous aggregates to the crystals with strictly defined translational symmetry in three directions. One-dimensional protein aggregates (amyloid fibrils) represent highly ordered semiflexible polymers with unique mesoscopic properties which can be tuned by both intrinsic physicochemical characteristics of polypeptide chain and milieu conditions. In the present work the molecular mechanisms of amyloid formation are discussed and mathematical description of the existing models of protein fibrillization are given. For disease-related amyloids, deeper understanding of fibril growth process may shed light on the pathogenesis and molecular mechanisms of the disorders, as well as on the strategies of amyloidosis prevention at atomistic level. In the context of nanotechnology and functional material science, knowing the details of amyloid formation is crucially required for the design of novel nanomaterials with unprecedented qualities. |
topic |
amyloid fibrils misfolding mathematical models amyloid diseases nanomaterials |
url |
http://periodicals.karazin.ua/eejp/article/view/10463 |
work_keys_str_mv |
AT vtrusova modelizationofamyloidfibrilselfassembly AT ggorbenko modelizationofamyloidfibrilselfassembly |
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1725454620125298688 |