BIOSENSORS & BIOELECTRONICS
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2013
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IF 5.437
Liping Liang,Yijuan Long,Haijie Zhang,Qinlong Wang,Xiaoxiao Huang,Rui Zhu,Ping Teng,Xiliang Wang,Huzhi Zheng
Two complementary colors mixed in a proper proportion will produce a neutral color in the color theory. A novel colorimetric method on basis of the color complementarity principle has been well-established to detect recombinant prion protein (rPrP). We found that a colorless solution appeared after mixing orange CdTe quantum dots (QDs) with green-blue malachite green (MG) because of color complementarity. After the addition of rPrP into the mixed solution, the color changed from colorless to green-blue because rPrP could induce the aggregation of QDs, rapidly. And it could be observed by naked eyes. Based on this phenomenon, we developed a simple assay for visual detection of rPrP. At the same time, we obtained excellent correlation between absorption and concentrations of rPrP from 1 nmol L −1 to 78 nmol L −1 with the limit of detection of 0.3 nmol L −1 (3 σ ). Moreover, it can be applied to determine rPrP in human serum successfully. Importantly, this assay possesses the advantages of simplicity, rapidity, sensitivity, and selectivity, and shows the potential in the clinical diagnostic test of early prion disease and provides the possibility of preventing the spread of prion diseases.
研究领域:
生物化学
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医学诊断
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纳米技术
✓ 已验证
产品关联
DOI
PubMed
高影响因子
TALANTA
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2011
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IF 3.722
Hai-Jie Zhang,Hu-Zhi Zheng,Yi-Juan Long,Geng-Fu Xiao,Ling-Yan Zhang,Qin-Long Wang,Mei Gao,Wen-Jun Bai
Because amyloidogenic proteins, such as prion protein, β-amyloid peptide and α-synuclein, are associated with a variety of diseases, methods for their detection are important. Recombinant prion protein (rPrP) can selectively induce aggregation of dihydrolipoic acid capped gold nanoparticles (DHLA-AuNPs), which reduces the absorbance of the DHLA-AuNPs and changes their color from red to blue. These changes were used for label-free qualitative and quantitative detection of amyloidogenic protein. The addition of NaCl improved the detection sensitivity considerably, and the detection limit was as low as 33 pmol/L.
研究领域:
生物化学
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医学诊断
✓ 已验证
产品关联
DOI
PubMed
高影响因子
Science Advances
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2025
·Vol. 11
·期 32
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IF 12.5
Runchuan Yan,Yan Zhang,Jingjing Zhang,Xiangyi Zhang,Yue Han,Mengfei Wang,Dan Wang,Shengnan Huang,Wei Liu,Qi Shi,Xiaoping Dong,Wen-Quan Zou,Zhen Li,Jiyan Ma
Rapid neurodegeneration distinguishes prion disease from other neurodegenerative disorders. Notably, normal prion protein (PrP C ) is essential for prion-induced rapid neurodegeneration, but the underlying mechanism remains unknown. Here, we show that the unstructured N-terminal region of PrP C induces rapid and lethal neurodegeneration in mice, accompanied by the hallmark of prion disease, spongiosis. The neurotoxic N-terminal PrP is soluble, associates peripherally with lipid membranes, and induces neurotoxicity only when a critical threshold is exceeded. Both the N-terminally localized KKRPKP sequence and octarepeats contribute to neurotoxicity, with KKRPKP being essential. Without it, the N-terminal PrP is innocuous but exacerbates either neurodegeneration caused by N-terminal PrP or neurodegeneration in prion disease induced by intracerebral prion inoculation in mice. Our findings establish that soluble N-terminal PrP causes rapid neurodegeneration in prion disease and is a target for intervention.
研究领域:
神经生物学
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分子生物学
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病理学
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转化医学
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蛋白质错误折叠疾病
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产品关联
DOI
PubMed
高影响因子
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
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2021
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IF 6.953
Chunjun Yan,Zheng Zhou
Prion diseases are fatal neurodegenerative diseases caused by the conformational transition of the cellular prion protein (PrP C ) to the abnormal pathological prion protein (PrP Sc ). In this work, the effects of ellagic acid (EA) and pentagalloylglucose (PGG) on prion protein (PrP) fibrillization were investigated. Fluorescence quenching experiments indicated that both EA and PGG could specifically interact with native human PrP with binding affinities of 1.92 × 10 5 and 2.36 × 10 5 L·mol −1 , respectively. Thioflavin-T (ThT) fluorescence assays showed that the binding of EA or PPG could effectively inhibit the nucleation and elongation of PrP fibrilization and reduce the amount of PrP fibrils generated. EA and PGG could also lead to a significant disaggregation of PrP fibrils. Circular dichroism (CD) measurements suggested that EA- or PPG-bound PrP could preserve a higher content of α-helical structures than β-sheet-rich PrP fibrils. The PrP aggregates formed in the presence of EA or PGG showed lower resistance to proteinase K (PK) digestion. Overall, the present work reported the inhibitory effect of EA and PGG on PrP fibrillization. These two natural polyphenols could be potential prodrug molecules for the prevention and treatment of prion diseases.
研究领域:
神经科学
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生物化学
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药理学
✓ 已验证
产品关联
DOI
PubMed
高影响因子
Journal of Analysis and Testing
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2025
·
IF 7
Lv Yubing,Zhou Yanli,Lv Chaoran,Wang Mengyao,Sheng Nan,Lin Yuanyuan,Wang Cancan,Xu Maotian,Zhang Jing,Yan Mei
In view of the importance of quantification of beta-amyloid (Aβ), an “aptamer -target- peptide” sandwich electrochemical biosensor to assay Aβ42 was fabricated by using gold–palladium bimetallic nanoparticles covalent organic framework-carbon cloth (Au–Pd@COF TTF-Thi -CC) and prion protein (PrP C ) labeled with horseradish peroxidase (HRP) nanocomposites. The concentration of Aβ42 showed a positive correlation with the peak current resulting from the oxidation of hydroquinone (HQ) by HRP. In contrast, the reference current signal from thionin (Thi), derived from covalent organic framework (COF), showed a negative correlation. The current response of the electrochemical biosensor was proportional to the Aβ concentrations ranging from 0.01 to 2.5 nM with a detection limit (LOD) of 2.17 fM ( S / N = 3). The sensitivity of the sandwich electrochemical biosensor could be primarily amplified based on the substrates of Au–Pd@COF TTF-Thi -CC. The AuNPs and PdNPs not only facilitated the bonding of the linker based on the Au–S bond but also improved the performance of COF TTF-Thi -CC. Secondary sensitivity amplification of the biosensor could be achieved by using PrP C -labeled HRP to catalyze hydroquinone in solution. Furthermore, the biosensor showed excellent selectivity, anti-interference performance, and stability. The Aβ concentrations in cerebrospinal fluid (CSF) were successfully evaluated using the constructed biosensor. This assay provides a potential tool for early-stage Alzheimer's disease diagnosis.
研究领域:
生物传感器
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纳米技术
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神经化学
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电化学
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分析化学
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阿尔茨海默病研究
✓ 已验证
产品关联
DOI
高影响因子
危险品化学品经营许可证（带存储）