Inhibition of Alzheimer amyloid β aggregation by polyvalent trehalose

Miura, Yoshiko; You, Chouga; Ohnishi, Reiko

doi:10.1088/1468-6996/9/2/024407

Cited by 19 publications

(27 citation statements)

References 28 publications

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“…The atypical aggregation and fixation of individual proteins takes place in patients with any of the above diseases. A study demonstrated that trehalose decreases such effects and inhibits formation of neurotoxic amyloids (Liu et al 2005 ; Miura et al 2008 ; Yu et al 2012 ; Chaudhary et al 2014 ).…”

Section: Industrial Application Of Trehalosementioning

confidence: 99%

Propionibacterium spp.—source of propionic acid, vitamin B12, and other metabolites important for the industry

Piwowarek

Lipińska

Hać‐Szymańczuk

et al. 2017

Appl Microbiol Biotechnol

169

104

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Bacteria from the Propionibacterium genus consists of two principal groups: cutaneous and classical. Cutaneous Propionibacterium are considered primary pathogens to humans, whereas classical Propionibacterium are widely used in the food and pharmaceutical industries. Bacteria from the Propionibacterium genus are capable of synthesizing numerous valuable compounds with a wide industrial usage. Biomass of the bacteria from the Propionibacterium genus constitutes sources of vitamins from the B group, including B12, trehalose, and numerous bacteriocins. These bacteria are also capable of synthesizing organic acids such as propionic acid and acetic acid. Because of GRAS status and their health-promoting characteristics, bacteria from the Propionibacterium genus and their metabolites (propionic acid, vitamin B12, and trehalose) are commonly used in the cosmetic, pharmaceutical, food, and other industries. They are also used as additives in fodders for livestock. In this review, we present the major species of Propionibacterium and their properties and provide an overview of their functions and applications. This review also presents current literature concerned with the possibilities of using Propionibacterium spp. to obtain valuable metabolites. It also presents the biosynthetic pathways as well as the impact of the genetic and environmental factors on the efficiency of their production.

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Section: Industrial Application Of Trehalosementioning

confidence: 99%

Propionibacterium spp.—source of propionic acid, vitamin B12, and other metabolites important for the industry

Piwowarek

Lipińska

Hać‐Szymańczuk

et al. 2017

Appl Microbiol Biotechnol

169

104

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“…From the chemical view point, because trehalose is a non-reducing saccharide, it is relatively stable for chemical reactions. 3 Due to the chemical stability and the symmetry of the structure, trehalose is useful as a building block of polymers; 3 and our research group 4–8 and other groups 9–16 have synthesized various types of polymers from trehalose. Srinivasachari et al 13 and Anderson et al 14 developed low toxic trehalose-based cationic polymers for effective gene delivery.…”

Section: Introductionmentioning

confidence: 99%

“…Srinivasachari et al 13 and Anderson et al 14 developed low toxic trehalose-based cationic polymers for effective gene delivery. Miura et al 15,16 reported the suppression of Alzheimer amyloid aggregation by a glycopolymer carrying trehalose as pendant groups. Mancini et al 12 reported that the glycopolymer carrying trehalose could stabilize a protein to lyophilization and heat.…”

Section: Introductionmentioning

confidence: 99%

Fibroblast cell proliferation on photo-cured trehalose cinnamoyl ester thin films

Yano

Teramoto

Miyamoto

et al. 2014

Journal of Bioactive and Compatible Polymers

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Trehalose cinnamoyl esters (TCs) were synthesized by esterification of trehlaose with cinnamoyl chloride. Two TCs with different degrees of substitution were synthesized, and trehalose cinnamoyl ester thin film-coated glass plates were prepared by a dip-coating method. Photocuring of the TCs was confirmed by ultraviolet–visible spectral changes. The surface of photo-cured TCs were found smooth as observed in a scanning electron microscope. The cell proliferation on the photo-cured TCs was investigated using 3T3 Swiss Albino mouse embryo fibroblasts. The results of the cell proliferation assay revealed that the photo-cured TCs with higher degrees of substitution promoted the cell proliferation compared with a polystyrene culture plate and the photo-cured TCs with lower degrees of substitution. The contact angle of the photo-cured TCs with higher degrees of substitution was 101.0° ± 1.6°, which is much higher than that of the polystyrene culture plate, and it is out of the range known to be suitable for cell adhesion. Nevertheless, the cell unexpectedly grew best on the photo-cured TCs with higher degrees of substitution. Fibronectin binding assay was carried out using fluorescent probe-modified fibronectin, and more fibronectin was found adsorbed onto photo-cured TCs than a polystyrene culture plate.

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“…Plaques are, in part, composed of masses of filaments, which are in turn composed of the insoluble form of the Aβ peptide [5,39,40]. These Aβ aggregates may cause neuronal injury directly by acting on synapses, or indirectly by activating microglia and astrocytes and therefore pharmacological interventions have been developed to target the sequential events originating from Aβ synthesis [40,41]. Usually neuritic plaques composed of amyloid β-protein (Aβ) are an early and invariant neuropathological feature of Alzheimer's disease (AD), [41].…”

Section: The Alzheimer's Diseasementioning

confidence: 99%

“…These Aβ aggregates may cause neuronal injury directly by acting on synapses, or indirectly by activating microglia and astrocytes and therefore pharmacological interventions have been developed to target the sequential events originating from Aβ synthesis [40,41]. Usually neuritic plaques composed of amyloid β-protein (Aβ) are an early and invariant neuropathological feature of Alzheimer's disease (AD), [41]. Genetic and neuropatho logical studies suggest that the processing of amyloid precursor protein (APP) to yield amyloid β-protein (Aβ), and its subsequent aggregation, play important roles in the pathogenesis of Alzheimer's disease (AD) as the numbers of A plaques and A burden increased over time in the brain with AD and A deposition precedes clinical symptom of AD.…”

Section: The Alzheimer's Diseasementioning

confidence: 99%

Review: structure of amyloid fibril in diseases

Ghahghaei¹,

Faridi²

2009

JBiSE

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Tissue deposition of normally soluble proteins, or their fragments, as insoluble amyloid fibrils causes both acquired and hereditary systemic amyloidoses, which is usually fatal. Amyloid is associated with serious diseases such as Alzheimer's disease, type 2 diabetes, Parkinson's Disease, Huntington's Disease, cancer and the transmissible spongiform encephalopathies. Information concerning the structure and mechanism of formation of fibrils in these diseases is critical for understanding the process of pathology of the amyloidoses and to the development of more effective therapeutic agents that target the underlying disease mechanisms. Structural models have been made using information from a wide variety of techniques, including electron microscopy, X-ray diffraction, solid state NMR, and Congo red and CD spectroscopy. Although each type of amyloidosis is characterised by a specific amyloid fibril protein, the deposits share pathognomonic histochemical properties and the structural morphology of all amyloid fibrils is very similar. In fact, the structural similarity that defines amyloid fibres exists principally at the level of β-sheet folding of the polypeptides within the protofilament, while the different types vary in the supramolecular assembly of their protofilaments.

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Inhibition of Alzheimer amyloid β aggregation by polyvalent trehalose

Cited by 19 publications

References 28 publications

Propionibacterium spp.—source of propionic acid, vitamin B12, and other metabolites important for the industry

Propionibacterium spp.—source of propionic acid, vitamin B12, and other metabolites important for the industry

Fibroblast cell proliferation on photo-cured trehalose cinnamoyl ester thin films

Review: structure of amyloid fibril in diseases

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