Abstract
Prion protein (PrPSc) has drawn widespread attention due to its pathological potential to prion diseases. In this work, we constructed a novel surface plasmon resonance (SPR) detection assay involving magnetic microspheres (MMs) and its controlled release property, for selective capture, embedding, concentration, and SPR detection of PrPSc with high sensitivity and specificity. Aptamer-modified magnetic particles (AMNPs) were used to specifically capture PrPSc. Amphiphilic copolymer was used to embed the labeled PrPSc and form magnetic microspheres to isolate PrPSc from the external environment. Static magnetic and alternating magnetic fields were used to concentrate and control release the embedded PrPSc, respectively. Finally, the released AMNPs-labeled PrPSc was detected by SPR which was equipped with a bare gold sensing film. A good linear relationship was obtained between SPR responses and the logarithm of PrPSc concentrations over a range of 0.01–1000 ng/mL. The detection sensitivity for PrPSc was improved by 10 fold compared with SPR direct detection format. The specificity of the present biosensor was also determined by PrPC and other reagents as controls. This proposed approach could also be used to isolate and detect other highly pathogenic biomolecules with similar structural characteristics by altering the corresponding aptamer in the AMNPs conjugates.
Highlights
Prion protein (PrPSc) has drawn widespread attention due to its pathological potential to prion diseases, such as Creutzfeldt Jakob syndrome and BSE [1]
It is clearly observed that the size distribution obtained from transmission electron microscopy (TEM) is 14.53 ± 0.08 nm, which is much smaller than the dimensions of Aptamer-modified magnetic particles (AMNPs) observed by AFM (23.29 ± 0.56 nm)
The saturation magnetization values are 65.37, 53.20 and 32.24 emu/g. These results indicate that the magnetic microspheres dispersed in the solution have a rapid response in a static magnetic field, and the orientational enrichment of the imbedded PrPSc can be achieved in a short time
Summary
Prion protein (PrPSc) has drawn widespread attention due to its pathological potential to prion diseases, such as Creutzfeldt Jakob syndrome and BSE [1]. There is an urgent need to develop a detection method of PrPSc for early diagnosis, which should be safe, sensitive and specific. More and more researches have introduced SPR as a potential powerful tool for the detection of PrPSc and PrPC [7,8,9]. It is reported that the minimum lethal dose of PrPSc in hamsters is less than 2 nM; the current sensitivity is not high enough for early diagnosis of prion disease [10]. Due to the low molecular weight (23 kDa) and the trace amount of PrPSc mixed with the large volume of circulating blood, it is highly important for the creation of a novel SPR-based detection assay for the PrPSc detection with ultra-sensitivity and high-specificity. Several approaches involving nanotechnology have been reported to enhance the SPR signals constructing a “sandwich” detection system [11,12]
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
