Metal-assisted core-shell plasmonic nanoparticles for small molecule biothiol analysis and enantioselective recognition.
Meihuang ZengLinmin ChenXiaocong HouJingwen JinQiuhong YaoTingxiu YeZhiyong GuoXiaomei ChenXi ChenPublished in: Nanoscale (2024)
Cysteine (Cys) enantiomorphs, important small-molecule biothiols, participate in various antioxidative, flavoring, and poison-removing processes in the food industry. Current cysteine enantiomorph analysis methods require effective strategies for distinguishing them due to their similar structures and reactivity. Herein, we present a metal ion-assisted enantiomorph-selective surface-enhanced Raman scattering (SERS) biosensor based on an amphiphilic polymer matrix (APM), which can promote cysteine enantiomorph (L/D-Cys) identification. The highly selective molecular orientation is perhaps caused by the intermolecular hydrogen bonding with chiral isomers (metal centers). The experimental results show that the SERS biosensor has a sensitivity-distincting factor toward L-Cys and D-Cys. The linear range is from 1 mmol L -1 to 1 nmol L -1 , along with a low limit of detection of 0.77 pmol L -1 . Moreover, the fabricated Cu-APM biosensor exhibits remarkable stability and high repeatability, with an RSD of 3.7%. Real food cysteine enantiomorph detection was performed with L-Cys-containing samples of onion, cauliflower, garlic, and apple, and D-Cys-containing samples of vinegar, black garlic, cheese, and beer. The results show that the Cu-APM biosensor can be utilized as a powerful tool for real-time determination of Cys enantiomorphs in different food samples. Thus, the metal-ion-assisted enantiomorph-selective SERS biosensor has potential as an adaptable tool for enantiomorph detection and food sample analysis.
Keyphrases
- label free
- sensitive detection
- gold nanoparticles
- small molecule
- loop mediated isothermal amplification
- fluorescent probe
- quantum dots
- human health
- living cells
- raman spectroscopy
- risk assessment
- climate change
- mass spectrometry
- protein protein
- ionic liquid
- energy transfer
- simultaneous determination
- bioinformatics analysis
- liquid chromatography