Protein nanofibrils and their use as building blocks of sustainable materials

RSC Advances, Год журнала: 2021, Номер 11(62), С. 39188 - 39215

Опубликована: Янв. 1, 2021

Protein nanofibrils produced from renewable resources provide opportunities to create novel materials for sustainable development.

Язык: Английский

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Functional Mammalian Amyloids and Amyloid-Like Proteins

Life, Год журнала: 2020, Номер 10(9), С. 156 - 156

Опубликована: Авг. 21, 2020

Amyloids are highly ordered fibrous cross-β protein aggregates that notorious primarily because of association with a variety incurable human and animal diseases (termed amyloidoses), including Alzheimer’s disease (AD), Parkinson’s (PD), type 2 diabetes (T2D), prion diseases. Some amyloid-associated diseases, in particular T2D AD, widespread affect hundreds millions people all over the world. However, recently it has become evident many amyloids, termed “functional amyloids,” involved various activities beneficial to organisms. Functional amyloids were discovered diverse taxa, ranging from bacteria mammals. These vital biological functions such as long-term memory, storage peptide hormones scaffolding melanin polymerization animals, substrate attachment, biofilm formation fungi, etc. Thus, undoubtedly playing important roles pathological processes. This review is focused on functional mammals summarizes approaches used for identifying new potentially amyloidogenic proteins domains.

Язык: Английский

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Current Understanding of the Structure, Stability and Dynamic Properties of Amyloid Fibrils

International Journal of Molecular Sciences, Год журнала: 2021, Номер 22(9), С. 4349 - 4349

Опубликована: Апрель 21, 2021

Amyloid fibrils are supramolecular protein assemblies represented by a cross-β structure and fibrous morphology, whose structural architecture has been previously investigated. While amyloid basically main-chain-dominated consisting of backbone hydrogen bonds, side-chain interactions also play an important role in determining their detailed structures physicochemical properties. In comprising short peptide segments, steric zipper where pair β-sheets with side chains interdigitate tightly is found as fundamental motif. longer polypeptides, each polypeptide chain folds into planar composed several β-strands linked turns or loops, the zippers formed locally to stabilize structure. Multiple segments capable forming contained within single molecule many cases, polymorphism appears result diverse regions counterparts zippers. Furthermore, β-solenoid structure, solenoid shape packed inside, recognized another primarily achieved non-polar residues disease-related fibrils, participation hydrophilic charged prominent functional amyloids, which often leads spatiotemporally controlled fibrillation, high reversibility, formation labile amyloids kinked topology. Achieving precise control will open up new horizon for designing useful amyloid-based nanomaterials.

Язык: Английский

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Structural analysis of cross α-helical nanotubes provides insight into the designability of filamentous peptide nanomaterials

Nature Communications, Год журнала: 2021, Номер 12(1)

Опубликована: Янв. 18, 2021

Abstract The exquisite structure-function correlations observed in filamentous protein assemblies provide a paradigm for the design of synthetic peptide-based nanomaterials. However, plasticity quaternary structure sequence-space and lability helical symmetry present significant challenges to de novo structural analysis such filaments. Here, we describe rational approach self-assembling peptide nanotubes based on controlling lateral interactions between protofilaments having an unusual cross-α supramolecular architecture. Near-atomic resolution cryo-EM seven designed provides insight into designability interfaces within these identifies non-native interaction pair arginine residues. This clasp motif can robustly mediate cohesive nanotubes. resultant be controlled through sequence length subunits, which generates filaments similar dimensions flagella pili.

Язык: Английский

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On the Structural Diversity and Individuality of Polymorphic Amyloid Protein Assemblies

Journal of Molecular Biology, Год журнала: 2021, Номер 433(20), С. 167124 - 167124

Опубликована: Июль 2, 2021

Язык: Английский

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