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1.
J Hazard Mater ; 474: 134596, 2024 Aug 05.
Article de Anglais | MEDLINE | ID: mdl-38820744

RÉSUMÉ

Because of the significant environmental and health hazards imposed by di(2-ethylhexyl) phthalate (DEHP), a common plasticizer, developing safe and green techniques to degrade DEHP plasticizer is of huge scientific significance. It has been observed that environmental contamination of DEHP may also induce serious food safety problems because crops raised in plasticizers contaminated soils would transfer the plasticizer into foods, such as Baijiu. Additionally, when plastic packaging or vessels are used during Baijiu fermentation and processing, plasticizer compounds frequently migrate and contaminate the product. In this study, hairpin-like structured peptides with catalytically active sites containing serine, histidine and aspartic acid were found to degrade DEHP. Furthermore, after incorporating caffeic acid molecules at the N-terminus, the peptides could be attached onto foam titanium (Ti) surfaces via enediol-metal interactions to create an enzyme-mimicking flow reactor for the degradation of DEHP in Baijiu. The structure and catalytic activity of peptides, their interaction with DEHP substrate and the hydrolysis mechanism of DEHP were discussed in this work. The stability and reusability of the peptide-modified foam Ti flow reactor were also investigated. This approach provides an effective technique for the degradation of plasticizer compounds.


Sujet(s)
Phtalate de bis[2-éthylhexyle] , Peptides , Plastifiants , Titane , Phtalate de bis[2-éthylhexyle]/composition chimique , Phtalate de bis[2-éthylhexyle]/métabolisme , Plastifiants/composition chimique , Titane/composition chimique , Peptides/composition chimique , Peptides/métabolisme , Hydrolyse
2.
J Mater Chem B ; 10(47): 9878-9886, 2022 12 07.
Article de Anglais | MEDLINE | ID: mdl-36437799

RÉSUMÉ

The self-assembly of a series of catalytically active polypeptides toward hydrolysis of glucoside compounds, namely, gastrodin, polydatin and esculin was investigated. These active peptides are composed of two functional fragments: one is the hydrophobic sequence LHLHLRL, which forms assembling segments in the presence of Zn ions (Zn2+); another functional sequence of active peptides are catalytic sites such as Glu (E), Asp (D) and His (H), where carboxylic acids (-COOH) or imidazole groups act like scissors to cleave glucoside bonds of the compounds (according to the acid-base coupling mechanism). The effects of the amino acid sequence of the peptide, Zn2+ concentration, pH and the size or steric hindrance of glucoside compounds on the hydrolytic activity were studied. It was found that the crystalline structure of assembled peptides was crucial to provide the peptide with catalytic hydrolytic activity. Noncovalent interaction index was used to analyse the noncovalent interaction of PEs with glucoside compounds, including hydrogen bonds, van der Waals, and steric effect in the complexes. The binding energy of complexes, the direction and site of nucleophilic attack during deglycosylation processes were also investigated by molecular docking and the electron density Laplace function. This revealed that the differences in the hydrolytic activity of peptides toward glucoside compounds with different sizes originated from different hydrogen bond interactions between the peptides and substrates. These active peptides may find application in the preparation of drugs by de-glycosylation of natural compounds.


Sujet(s)
Esculoside , Peptides , Simulation de docking moléculaire
3.
J Hazard Mater ; 428: 128262, 2022 04 15.
Article de Anglais | MEDLINE | ID: mdl-35051771

RÉSUMÉ

Organophosphorus pesticides (OPs) detection has attracted considerable attention because of the extensive application of OPs. In this research, non-toxic and high-performance metalloenzyme mimics of Zn2+-bonding peptides were developed by obtaining inspiration from phosphotriesterase (PTE) and nanofiber formation. Furthermore, based on the electrochemical activity of p-nitrophenol (PNP), the electrochemical sensor of metalloenzyme mimics was developed. By examining the effect of the active sites of peptides and fibril formation on the degradation of OPs, the optimal metalloenzyme mimic was selected. Furthermore, optimal metalloenzyme mimics were combined with NiCo2O4 to develop an electrochemical sensor of OPs. By monitoring square wave voltammetry (SWV) signals of PNP degraded from OPs, the amounts of OPs in actual samples could be determined in 15 min. We discovered that both the active sites of α metal and ß metal were required for metalloenzyme mimics; Zn2+ promoted peptide fibrosis and especially acted as a cofactor for degrading OPs. Compared to traditional methods, the electrochemical sensor of metalloenzyme mimics was sensitive, reliable, and non-toxic; furthermore, the detection limit of methyl paraoxon was as low as 0.08 µM. The metalloenzyme mimics will be a promising material for detecting OPs in the food industry and environment fields.


Sujet(s)
Techniques de biocapteur , Métalloprotéines , Pesticides , Composés organiques du phosphore , Peptides
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