Modulation of beta-amyloid aggregation using ascorbic acid

Sampaio, Isabella; Quatroni, Felipe Domingues; Lins, Paula Maria Pincela; Nascimento, Alessandro S.; Zucolotto, Valtencir

doi:10.1016/j.biochi.2022.05.006

Cited by 5 publications

(4 citation statements)

References 49 publications

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“…The negative signal at ≈220 nm of insulin and Aβ 42 aggregates indicated the formation of β‐sheet structure. [ 45 ] However, the signal at 220 nm obviously weakened in the presence of these three CDs, indicating the formation of lower β‐sheet structure. Additionally, in Figures 5C and 6C, insulin and Aβ 42 self‐assembly aggregates exhibited the classical fibril structure; however, when co‐incubated with the three individual CDs (200 µg mL −1 ), the formed amorphous protein aggregates were greatly smaller in the size compared to their respective self‐assembly aggregates.…”

Section: Resultsmentioning

confidence: 99%

Congo Red‐Derived Carbon Dots: Simultaneously as Fluorescence Probe for Protein Aggregates, Inhibitor for Protein Aggregation, and Scavenger of Free Radicals

et al. 2023

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β-sheet-rich protein aggregates. [2] Protein aggregates deposit in the specific organ or tissue is possibly the significant hallmark of some protein aggregation diseases. [3] For example, the Lewy bodies contain abundant α-synuclein aggregates in the brain of PD patients, [3] and the extracellular senile plaques comprise both of Aβ 1-40 (Aβ 40 ) and Aβ 1-42 (Aβ 42 ) aggregates in the brain of AD patients. [3,4] Specifically, for the AD-associated proteins, Aβ 42 is a more prevalent amyloidogenic protein in the senile plaques, exhibiting faster aggregation rate in vitro and higher neurotoxicity in vivo than Aβ 40 , [4][5][6][7] which is a widely-accepted model aggregative protein in the AD study. [8] The formed protein aggregates, especially the soluble oligomers and protofibrils, could pose high cytotoxicity, causing the damage of cell membrane, dysfunction of organelles (such as mitochondrion and golgi apparatus) as well as cellular oxidative stress with elevated free radical level. [9][10][11][12] Therefore, detection of protein aggregates, inhibition of protein aggregation, and scavenging of free radical would be of great significance for the diagnosis and treatment of the protein aggregation diseases. [13,14] However, it is still challenging to achieve the dual purposes of simultaneous detection and treatment in one method. [15,16] Fluorescence imaging method with the characteristics of being low invasive and real time was widely developed for diagnosis. [13,17] As one of high-profile carbon-based nanomaterials, carbon dots (CDs), with the merits of excellent fluorescence property, good biocompatibility, low cytotoxicity, easy preparation, and low cost, [18,19] were introduced for fluorescence imaging of protein aggregates. [20][21][22][23] However, the fluorescence signals of some CDs were in the blue or green emission range, which were easily interfered by the autofluorescence of biological samples. [24] In contrast, red fluorescence response possessing good anti-interference ability was more preferable. [24] Besides, owing to the size effects and plentiful surface functional groups, CDs aroused researchers' interests in their potential inhibition effects on protein aggregation, which could be a strategy to delay or reverse the diseases. [16] Previously, Gao et al. proposed nitrogen-doped carbonized polymer dots, whichThe pathological aggregation of some proteins is claimed to be highly related to several human diseases, such as β-amyloid 1-42 (Aβ 42 ) to Alzheimer's disease (AD), islet amyloid polypeptide, and insulin to type 2 diabetes mellitus. Therefore, it is in desperate need to develop effective methods for detection of protein aggregates and inhibition of abnormal aggregation. Herein, to construct all-in-one probe with both diagnosis and treatment potentials for protein aggregation diseases, Congo red (CR), a classical staining reagent with red fluorescence signal output for protein aggregates, is deliberately adopted to react with three different reductive carbon sources and ammonium persulfate to ...

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Section: Resultsmentioning

confidence: 99%

Congo Red‐Derived Carbon Dots: Simultaneously as Fluorescence Probe for Protein Aggregates, Inhibitor for Protein Aggregation, and Scavenger of Free Radicals

et al. 2023

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“…In the presence of these two metal ions, ascorbic acid loses its antioxidant properties, favoring the production of ROS species [ 124 ]. Moreover, ascorbic acid is able to tightly associate with Aβ and binds to Aβ42 oligomers at sites in the D23-K28 region [ 281 ]. In this respect, further investigations on ternary systems (Aβ, Cu(II), and vitamin C) may be useful to explain the chemical equilibria and the species forming in the solution.…”

Section: Discussionmentioning

confidence: 99%

Bioinorganic Chemistry of Micronutrients Related to Alzheimer’s and Parkinson’s Diseases

Kola,

Nencioni,

Valensin

2023

Molecules

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Metal ions are fundamental to guarantee the regular physiological activity of the human organism. Similarly, vitamins play a key role in many biological functions of the metabolism, among which are coenzymes, redox mediators, and antioxidants. Due to their importance in the human organism, both metals and vitamins have been extensively studied for their involvement in neurodegenerative diseases (NDs). However, the full potential of the interaction between vitamins and metal ions has not been fully explored by researchers yet, and further investigation on this topic is needed. The aim of this review is to provide an overview of the scientific literature on the implications of vitamins and selected metal ions in two of the most common neurodegenerative diseases, Alzheimer’s and Parkinson’s disease. Furthermore, vitamin–metal ion interactions are discussed in detail focusing on their bioinorganic chemistry, with the perspective of arousing more interest in this fascinating bioinorganic field.

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“…Care [16][17][18][19]). The possible effect of ascorbic acid on wound healing due to proliferative action [20] and the prevention of Alzheimer's disease due to the efficient binding of AAH 2 0 to amyloid-β oligopeptide [21] is also being studied.…”

Section: Introductionmentioning

confidence: 99%

Copper (II)-Catalyzed Oxidation of Ascorbic Acid: Ionic Strength Effect and Analytical Use in Aqueous Solution

Murekhina

Yarullin

Sovina³

et al. 2022

Inorganics

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Copper is an important metal both in living organisms and in the industrial activity of humans, it is also a distributed water pollutant and a toxic agent capable of inducing acute and chronic health disorders. There are several fluorescent chemosensors for copper (II) determination in solutions; however, they are often difficult to synthesize and solvent-sensitive, requiring a non-aqueous medium. The present paper improves the known analytical technique for copper (II) ions, where the linear dependence between the ascorbic acid oxidation rate constant and copper (II) concentration is used. The limits of detection and quantification of the copper (II) analysis kinetic method are determined to be 82 nM and 275 nM, respectively. In addition, the selectivity of the chosen indicator reaction is shown: Cu2+ cations can be quantified in the presence of the 5–20 fold excess of Co2+, Ni2+, and Zn2+ ions. The La3+, Ce3+, and UO22+ ions also do not catalyze the ascorbic acid oxidation reaction. The effect of the concentration of the common background electrolytes is studied, the anomalous influence for chloride-containing salts is observed and discussed.

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Modulation of beta-amyloid aggregation using ascorbic acid

Cited by 5 publications

References 49 publications

Congo Red‐Derived Carbon Dots: Simultaneously as Fluorescence Probe for Protein Aggregates, Inhibitor for Protein Aggregation, and Scavenger of Free Radicals

Congo Red‐Derived Carbon Dots: Simultaneously as Fluorescence Probe for Protein Aggregates, Inhibitor for Protein Aggregation, and Scavenger of Free Radicals

Bioinorganic Chemistry of Micronutrients Related to Alzheimer’s and Parkinson’s Diseases

Copper (II)-Catalyzed Oxidation of Ascorbic Acid: Ionic Strength Effect and Analytical Use in Aqueous Solution

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