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Amyloid: Structure and Function
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Amyloid: Structure and Function

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Informatics".

Deadline for manuscript submissions: closed (20 September 2022) | Viewed by 10584

Special Issue Editor

Dr. Vitaly V. Kushnirov

E-Mail Website
Guest Editor
Bach Institute of Biochemistry, Moscow, Russia
Interests: prion; amyloid; liquid-liquid phase separation (LLPS); mnemon; chaperones; Sup35; yeast; proteinase K
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Amyloids and their infective form, prions, occupy a special place in molecular biology; not central, but interesting and enigmatic. While DNA, RNA, and proteins were created by nature through natural selection, amyloids were not. They result from a side property – a kind of a flaw – of protein matter. Due to this, they mainly manifest as diseases. However, the nature can find use for any property, and there is already a fairly long list of useful mechanisms based on amyloids. The structure of amyloids is another interesting issue. In contrast to 3-D crystals formed by small molecules and globular proteins, amyloids are 1-dimensional crystals. While, during formation of 3-D crystals, the spatial freedom belongs to whole molecules, amyloids are formed by unfolded polypeptides in which every residue possesses some freedom before the amyloid structure is fixed. Amyloid formation in vitro requires just amyloidogenic protein, but in vivo, it is a complex process involving many other proteins, mainly chaperones.

According to the presented considerations, the main topics that will be the focus of this Special Issue are the process of in vivo amyloid formation, the structure of amyloids, and useful or potentially useful mechanisms based on amyloids and prions.

Dr. Vitaly V. Kushnirov
Guest Editor

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Keywords

  • Amyloid
  • Prion
  • Amyloid structure
  • Amyloid formation
  • Potentially useful mechanism

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Published Papers (3 papers)

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Research

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13 pages, 7835 KiB  
Article
Amyloid Properties of the FXR1 Protein Are Conserved in Evolution of Vertebrates
by Maria E. Velizhanina and Alexey P. Galkin
Int. J. Mol. Sci. 2022, 23(14), 7997; https://doi.org/10.3390/ijms23147997 - 20 Jul 2022
Cited by 4 | Viewed by 2094
Abstract
Functional amyloids are fibrillary proteins with a cross-β structure that play a structural or regulatory role in pro- and eukaryotes. Previously, we have demonstrated that the RNA-binding FXR1 protein functions in an amyloid form in the rat brain. This RNA-binding protein plays an [...] Read more.
Functional amyloids are fibrillary proteins with a cross-β structure that play a structural or regulatory role in pro- and eukaryotes. Previously, we have demonstrated that the RNA-binding FXR1 protein functions in an amyloid form in the rat brain. This RNA-binding protein plays an important role in the regulation of long-term memory, emotions, and cancer. Here, we evaluate the amyloid properties of FXR1 in organisms representing various classes of vertebrates. We show the colocalization of FXR1 with amyloid-specific dyes in the neurons of amphibians, reptiles, and birds. Moreover, FXR1, as with other amyloids, forms detergent-resistant insoluble aggregates in all studied animals. The FXR1 protein isolated by immunoprecipitation from the brains of different vertebrate species forms fibrils, which show yellow-green birefringence after staining with Congo red. Our data indicate that in the evolution of vertebrates, FXR1 acquired amyloid properties at least 365 million years ago. Based on the obtained data, we discuss the possible role of FXR1 amyloid fibrils in the regulation of vital processes in the brain of vertebrates. Full article
(This article belongs to the Special Issue Amyloid: Structure and Function)
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Review

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20 pages, 848 KiB  
Review
Structural Bases of Prion Variation in Yeast
by Vitaly V. Kushnirov, Alexander A. Dergalev, Maya K. Alieva and Alexander I. Alexandrov
Int. J. Mol. Sci. 2022, 23(10), 5738; https://doi.org/10.3390/ijms23105738 - 20 May 2022
Cited by 10 | Viewed by 3264
Abstract
Amyloids are protein aggregates with a specific filamentous structure that are related to a number of human diseases, and also to some important physiological processes in animals and other kingdoms of life. Amyloids in yeast can stably propagate as heritable units, prions. Yeast [...] Read more.
Amyloids are protein aggregates with a specific filamentous structure that are related to a number of human diseases, and also to some important physiological processes in animals and other kingdoms of life. Amyloids in yeast can stably propagate as heritable units, prions. Yeast prions are of interest both on their own and as a model for amyloids and prions in general. In this review, we consider the structure of yeast prions and its variation, how such structures determine the balance of aggregated and soluble prion protein through interaction with chaperones and how the aggregated state affects the non-prion functions of these proteins. Full article
(This article belongs to the Special Issue Amyloid: Structure and Function)
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18 pages, 4796 KiB  
Review
Amyloids as Building Blocks for Macroscopic Functional Materials: Designs, Applications and Challenges
by Jingyao Li and Fuzhong Zhang
Int. J. Mol. Sci. 2021, 22(19), 10698; https://doi.org/10.3390/ijms221910698 - 2 Oct 2021
Cited by 27 | Viewed by 4008
Abstract
Amyloids are self-assembled protein aggregates that take cross-β fibrillar morphology. Although some amyloid proteins are best known for their association with Alzheimer’s and Parkinson’s disease, many other amyloids are found across diverse organisms, from bacteria to humans, and they play vital functional roles. [...] Read more.
Amyloids are self-assembled protein aggregates that take cross-β fibrillar morphology. Although some amyloid proteins are best known for their association with Alzheimer’s and Parkinson’s disease, many other amyloids are found across diverse organisms, from bacteria to humans, and they play vital functional roles. The rigidity, chemical stability, high aspect ratio, and sequence programmability of amyloid fibrils have made them attractive candidates for functional materials with applications in environmental sciences, material engineering, and translational medicines. This review focuses on recent advances in fabricating various types of macroscopic functional amyloid materials. We discuss different design strategies for the fabrication of amyloid hydrogels, high-strength materials, composite materials, responsive materials, extracellular matrix mimics, conductive materials, and catalytic materials. Full article
(This article belongs to the Special Issue Amyloid: Structure and Function)
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