Aptamer-based silver nanosensor for multiple protein detection

Lab on a Chip ◽  
2012 ◽  
Vol 12 (17) ◽  
pp. 3184 ◽  
Author(s):  
Ying Wang ◽  
Danke Xu ◽  
Hong-Yuan Chen
Lab on a Chip ◽  
2020 ◽  
Vol 20 (12) ◽  
pp. 2113-2121 ◽  
Author(s):  
Kenji Akama ◽  
Hiroyuki Noji

Homogeneous digital immunoassay is a powerful analytical method for highly sensitive biomarker detection with a simple protocol. By using this method, we demonstrated the simultaneous multiple protein detection.


2015 ◽  
Vol 866 ◽  
pp. 1-9 ◽  
Author(s):  
Yuko Ueno ◽  
Kazuaki Furukawa ◽  
Kota Matsuo ◽  
Suzuyo Inoue ◽  
Katsuyoshi Hayashi ◽  
...  

The Analyst ◽  
2017 ◽  
Vol 142 (17) ◽  
pp. 3177-3182 ◽  
Author(s):  
Feiyang Wang ◽  
Yuexiang Lu ◽  
Jiacheng Yang ◽  
Ying Chen ◽  
Wenjie Jing ◽  
...  

We have developed a very simple colorimetric sensor array by using only unmodified gold nanoparticles and NaCl salt for discrimination of multiple proteins. The inexpensive and convenient sensor array and the ubiquitous smartphone are coupled to achieve an immediate point-of-care diagnosis without additional devices.


2015 ◽  
Vol 491 ◽  
pp. 31-36 ◽  
Author(s):  
Lin Cheng ◽  
Jie Zhang ◽  
Yan Lin ◽  
Qiong Wang ◽  
XiuXiu Zhang ◽  
...  

Bone ◽  
2020 ◽  
Vol 137 ◽  
pp. 115363
Author(s):  
Caterina Licini ◽  
Giorgia Montalbano ◽  
Gabriela Ciapetti ◽  
Giorgia Cerqueni ◽  
Chiara Vitale-Brovarone ◽  
...  

2011 ◽  
Vol 57 (12) ◽  
pp. 1732-1738 ◽  
Author(s):  
Jimin Zhu ◽  
Nengli Zou ◽  
Danian Zhu ◽  
Jin Wang ◽  
Qinghui Jin ◽  
...  

BACKGROUNDAlthough numerous lateral flow immunoassays (LFIAs) have been developed and widely used, inadequate analytical sensitivity and the lack of multiple protein detection applications have limited their clinical utility. We developed a new LFIA device for the simultaneous detection of high-sensitivity cardiac troponin I (hs-cTnI) and myoglobin (Myo).METHODSWe used a gold nanoparticle (AuNP) doubly labeled complex, in which biotinylated single-stranded DNA was used as a linkage to integrate 2 AuNPs and streptavidin-labeled AuNP, as an amplifier to magnify extremely low signals.RESULTSThe detection limit of 1 ng/L achieved for hs-cTnI was 1000 times lower than that obtained in a conventional LFIA. The detection limit for simultaneously measured Myo was 1 μg/L. The linear measurement ranges for hs-cTnI and Myo were 1–10 000 ng/L and 1–10 000 μg/L, respectively. We observed concordant results between the LFIA and clinical assays in sera from 12 patients with acute myocardial infarction (hs-cTnI r = 0.96; Myo r = 0.98). Assay imprecision was <11% for both hs-TnI and myo.CONCLUSIONSThe described proof-of-principle LFIA method could be used as a point-of-care device in multiple protein quantification and semiquantitative analysis.


2017 ◽  
Vol 14 (4) ◽  
pp. 393-402 ◽  
Author(s):  
Rajaraman Krishnan ◽  
Franz Hefti ◽  
Haim Tsubery ◽  
Michal Lulu ◽  
Ming Proschitsky ◽  
...  

Therapeutic strategies that target pathways of protein misfolding and the toxicity of intermediates along these pathways are mainly at discovery and early development stages, with the exception of monoclonal antibodies that have mainly failed to produce convincing clinical benefits in late stage trials. The clinical failures represent potentially critical lessons for future neurodegenerative disease drug development. More effective drugs may be achieved by pursuing the following two strategies. First, conformational targeting of aggregates of misfolded proteins, rather than less specific binding that includes monomer subunits, which vastly outnumber the toxic targets. Second, since neurodegenerative diseases frequently include more than one potential protein pathology, generic targeting of aggregates by shape might also be a crucial feature of a drug candidate. Incorporating both of these critical features into a viable drug candidate along with high affinity binding has not been achieved with small molecule approaches or with antibody fragments. Monoclonal antibodies developed so far are not broadly acting through conformational recognition. Using GAIM (General Amyloid Interaction Motif) represents a novel approach that incorporates high affinity conformational recognition for multiple protein assemblies, as well as recognition of an array of assemblies along the misfolding pathway between oligomers and fibers. A GAIM-Ig fusion, NPT088, is nearing clinical testing.


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