Oxygen Vacancy‐Engineered PEGylated MoO3−x Nanoparticles with Superior Sulfite Oxidase Mimetic Activity for Vitamin B1 Detection. Issue 46 (3rd October 2019)
- Record Type:
- Journal Article
- Title:
- Oxygen Vacancy‐Engineered PEGylated MoO3−x Nanoparticles with Superior Sulfite Oxidase Mimetic Activity for Vitamin B1 Detection. Issue 46 (3rd October 2019)
- Main Title:
- Oxygen Vacancy‐Engineered PEGylated MoO3−x Nanoparticles with Superior Sulfite Oxidase Mimetic Activity for Vitamin B1 Detection
- Authors:
- Chen, Yuan
Chen, Tongming
Wu, Xiaoju
Yang, Guowei - Abstract:
- Abstract: Sulfite oxidase (SuO x ) is a molybdenum‐dependent enzyme that catalyzes the oxidation of sulfite to sulfate to maintain the intracellular levels of sulfite at an appropriate low level. The deficiency of SuO x would cause severe neurological damage and infant diseases, which makes SuO x of tremendous biomedical importance. Herein, a SuO x mimic nanozyme of PEGylated (polyethylene glycol)‐MoO3 −x nanoparticles (P‐MoO3 −x NPs) with abundant oxygen vacancies created by vacancy‐engineering is reported. Their level of SuO x ‐like activity is 12 times higher than that of bulk‐MoO3 . It is also established that the superior increased enzyme mimetic activity is due to the introduction of the oxygen vacancies acting as catalytic hotspots, which allows better sulfite capture ability. It is found that vitamin B1 (VB1) inhibits the SuO x mimic activity of P‐MoO3 −x NPs through the irreversible cleavage by sulfite and the electrostatic interaction with P‐MoO3 −x NPs. A colorimetric platform is developed for the detection of VB1 with high sensitivity (the low detection limit is 0.46 µg mL −1 ) and good selectivity. These findings pave the way for further investigating the nanozyme which possess intrinsic SuO x mimicing activity and is thus a promising candidate for biomedical detection. Abstract : Oxygen vacancy engineering could effectively enhance the sulfite oxidase‐like (SuOx ) activity of PEGylated (polyethylene glycol)‐MoO3− x nanoparticles (P‐MoO3− x NPs) that catalyzeAbstract: Sulfite oxidase (SuO x ) is a molybdenum‐dependent enzyme that catalyzes the oxidation of sulfite to sulfate to maintain the intracellular levels of sulfite at an appropriate low level. The deficiency of SuO x would cause severe neurological damage and infant diseases, which makes SuO x of tremendous biomedical importance. Herein, a SuO x mimic nanozyme of PEGylated (polyethylene glycol)‐MoO3 −x nanoparticles (P‐MoO3 −x NPs) with abundant oxygen vacancies created by vacancy‐engineering is reported. Their level of SuO x ‐like activity is 12 times higher than that of bulk‐MoO3 . It is also established that the superior increased enzyme mimetic activity is due to the introduction of the oxygen vacancies acting as catalytic hotspots, which allows better sulfite capture ability. It is found that vitamin B1 (VB1) inhibits the SuO x mimic activity of P‐MoO3 −x NPs through the irreversible cleavage by sulfite and the electrostatic interaction with P‐MoO3 −x NPs. A colorimetric platform is developed for the detection of VB1 with high sensitivity (the low detection limit is 0.46 µg mL −1 ) and good selectivity. These findings pave the way for further investigating the nanozyme which possess intrinsic SuO x mimicing activity and is thus a promising candidate for biomedical detection. Abstract : Oxygen vacancy engineering could effectively enhance the sulfite oxidase‐like (SuOx ) activity of PEGylated (polyethylene glycol)‐MoO3− x nanoparticles (P‐MoO3− x NPs) that catalyze the oxidation of sulfite to sulfate. … (more)
- Is Part Of:
- Small. Volume 15:Issue 46(2019)
- Journal:
- Small
- Issue:
- Volume 15:Issue 46(2019)
- Issue Display:
- Volume 15, Issue 46 (2019)
- Year:
- 2019
- Volume:
- 15
- Issue:
- 46
- Issue Sort Value:
- 2019-0015-0046-0000
- Page Start:
- n/a
- Page End:
- n/a
- Publication Date:
- 2019-10-03
- Subjects:
- oxygen vacancy‐engineered -- P‐MoO3−x NPs -- sulfite oxidase mimetic -- vitamin B1 detection
Nanotechnology -- Periodicals
Nanoparticles -- Periodicals
Microtechnology -- Periodicals
620.5 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1613-6829 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/smll.201903153 ↗
- Languages:
- English
- ISSNs:
- 1613-6810
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 8309.952000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 15265.xml