Exploring the influence of brilliant blue G on amyloid fibril formation of lysozyme

How, Su-Chun; Hsin, Ai; Chen, Guan-Yu; Hsu, Wu‐Huei; Yang, Szu-Ming; Chou, Wei‐Lung; Chou, Shang‐Shing P.; Wang, Steven S.‐S.

doi:10.1016/j.ijbiomac.2019.07.055

Cited by 12 publications

(4 citation statements)

References 66 publications

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“…As can be established by testing various sequences on the above servers (we focused on AmyloGram [74,96], see later), as well as the classical amyloidoses, a very great many [120][121][122] (and possibly most [123]) proteins can exhibit amyloid formation under certain conditions [65,124]. Examples include insulin [125][126][127], lysozyme [128][129][130][131][132][133][134][135][136], proteins providing structure/texture in various processed foods and other gels [137-139], and even certain yeast [140][141][142] and bacterial [143] proteins, including some that can be 'inherited'.…”

Section: Prevalence Of Amyloidogenicitymentioning

confidence: 99%

Proteomic evidence for amyloidogenic cross-seeding in fibrinaloid microclots

Kell,

Pretorius

2024

Preprint

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In classical amyloidoses, amyloid fibres form through the nucleation and accretion of protein monomers, with protofibrils and fibrils exhibiting a cross-β motif of parallel or antiparallel β-sheets oriented perpendicular to the fibre direction. These protofibrils and fibrils can intertwine to form mature amyloid fibres. Similar phenomena occur in blood from individuals with circulating inflammatory molecules (also those originating from viruses and bacteria). In the presence of inflammagens, pathological clotting can occur, that results in an anomalous amyloid form termed fibrinaloid microclots. Previous proteomic analyses of these microclots have shown the presence of non-fibrin(ogen) proteins, suggesting a more complex mechanism than simple entrapment. We provide evidence against a simple entrapment model, noting that clot pores are too large and centrifugation would have removed weakly bound proteins. Instead, we explore whether co-aggregation into amyloid fibres may involve axial (multiple proteins within the same fibril), lateral (single-protein fibrils contributing to a fibre), or both types of integration. Our analysis of proteomic data from fibrinaloid microclots in different diseases shows no significant overlap with the normal plasma proteome and no correlation between plasma protein abundance and presence in microclots. Notably, abundant plasma proteins like α-2-macroglobulin, fibronectin, and transthyretin are absent from microclots, while less abundant proteins such as adiponectin, periostin, and von Willebrand Factor are well represented. Using bioinformatic tools including AmyloGram and AnuPP, we found that proteins entrapped in fibrinaloid microclots exhibit high amyloidogenic tendencies, suggesting their integration as cross-β elements into amyloid structures. This integration likely contributes to the microclots’ resistance to proteolysis. Our findings underscore the role of cross-seeding in fibrinaloid microclot formation and highlight the need for further investigation into their structural properties and implications in thrombotic and amyloid diseases. These insights provide a foundation for developing novel diagnostic and therapeutic strategies targeting amyloidogenic cross-seeding in blood clotting disorders.

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Section: Prevalence Of Amyloidogenicitymentioning

confidence: 99%

Proteomic evidence for amyloidogenic cross-seeding in fibrinaloid microclots

Kell,

Pretorius

2024

Preprint

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“…For example, BBG can bind to and inhibit various proteins [112] including other P2X receptors, albeit with lower efficacy than P2X7 [110,113]. In addition, BBG can inhibit the ATP-release channel pannexin-1 [114] and neuronal voltage-gated Na + channels [115], and it can also impair prion activity [116] and amyloid fibril formation [117] and conversely promote α-synuclein aggregation [118]. Thus, effects on P2X7 need to be confirmed using more specific compounds.…”

Section: Selection Of Antagonistsmentioning

confidence: 99%

Animal Models for the Investigation of P2X7 Receptors

Sluyter

Adriouch

Fuller

et al. 2023

IJMS

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The P2X7 receptor is a trimeric ligand-gated cation channel activated by extracellular adenosine 5′-triphosphate. The study of animals has greatly advanced the investigation of P2X7 and helped to establish the numerous physiological and pathophysiological roles of this receptor in human health and disease. Following a short overview of the P2X7 distribution, roles and functional properties, this article discusses how animal models have contributed to the generation of P2X7-specific antibodies and nanobodies (including biologics), recombinant receptors and radioligands to study P2X7 as well as to the pharmacokinetic testing of P2X7 antagonists. This article then outlines how mouse and rat models have been used to study P2X7. These sections include discussions on preclinical disease models, polymorphic P2X7 variants, P2X7 knockout mice (including bone marrow chimeras and conditional knockouts), P2X7 reporter mice, humanized P2X7 mice and P2X7 knockout rats. Finally, this article reviews the limited number of studies involving guinea pigs, rabbits, monkeys (rhesus macaques), dogs, cats, zebrafish, and other fish species (seabream, ayu sweetfish, rainbow trout and Japanese flounder) to study P2X7.

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“…Lysozyme (Ly) is widely present in mammalian blood, milk, saliva and various tissues (How et al, 2019). The relative molecular mass of Ly is about 14000, and it often exists as a white or slightly white freeze-dried powder.…”

Section: Introductionmentioning

confidence: 99%

Interaction investigation and phase transition of carrageenan/lysozyme complex system

et al. 2022

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Phase transition of lysozyme/carrageenan (Ly/CRG) complex system with different ratios, pH, ionic strength and temperature conditions was explored through ultraviolet-visible spectrophotometer, fluorescence spectrophotometer, fluorescence microscope, Zeta potential. The results showed that the main force between Ly and CRG is electrostatic interaction, and the Ly/CRG composite system has undergone three phase transition states: co-solubilization, gelation and aggregation. At pH = 1-3, the oppositely charged CRG and Ly form complexes based on electrostatic interaction. Whereas at pH = 12, both CRG and Ly are negatively charged and they repel each other electrostatically. The electrostatic shielding effect of salt ions had a greater impact on the formation of Ly/CRG complex. Temperature had a certain degree of influence on the structure and turbidity of the composite system. The interaction between polysaccharides and proteins can have a significant impact on the structure and stability of complex systems and the study of polysaccharide and protein complexes which will help to expand their application in food and medicine.

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Exploring the influence of brilliant blue G on amyloid fibril formation of lysozyme

Cited by 12 publications

References 66 publications

Proteomic evidence for amyloidogenic cross-seeding in fibrinaloid microclots

Proteomic evidence for amyloidogenic cross-seeding in fibrinaloid microclots

Animal Models for the Investigation of P2X7 Receptors

Interaction investigation and phase transition of carrageenan/lysozyme complex system

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