Abstract
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.
Highlights
EAST EUROPEAN JOURNAL OF PHYSICSIntermolecular 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
Міжмолекулярні нековалентні взаємодії між білковими молекулами призводять до формування широкого спектру надмолекулярних ансамблів, структура яких коливається від невпорядкованих аморфних агрегатів до кристалів із чітко визначеною трансляційною симетрією у трьох напрямках
The impairment of cell functions by fibrillized proteins and their intermediates is causatively linked to the complex conformational behavior of these aggregates, which are distinguished by the presence of a core cross-β-sheet structure with β-strands orienting perpendicularly to the fibril long axis and β-sheets propagating in its direction
Summary
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. Связанных с различными патологиями, понимание процесса роста фибрилл может пролить свет на патогенез и молекулярные механизмы амилоидных заболеваний, а также на стратегии предупреждения амилоидоза на атомистическом уровне. The impairment of cell functions by fibrillized proteins and their intermediates is causatively linked to the complex conformational behavior of these aggregates, which are distinguished by the presence of a core cross-β-sheet structure with β-strands orienting perpendicularly to the fibril long axis and β-sheets propagating in its direction. Such molecular architecture is stabilized by the main-chain hydrogen bonding, ionic pairing, van der EEJP Vol.. The aim of the present contribution is to analyze the molecular basis for protein fibrillization, and overview some mathematical models proposed to describe the process of amyloid formation
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