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PXD041715

PXD041715 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleSmall polystyrene microplastics interferes with the breakdown of milk proteins during static in vitro simulated human gastric digestion
DescriptionHuman ingestion of microplastics (MPs) is common and inevitable due to the widespread contamination of food items, but implications on the gastric digestion of food proteins are still unknown. In this study, the interaction between pepsin and polystyrene (PS) MPs was uncovered by investigating its effect on enzyme activity and conformation while in a simulated human gastric environment. The impact on food digestion was also determined by monitoring the kinetics of protein hydrolysis through static in vitro gastric digestion of cow’s milk contaminated with PS. The binding of pepsin to PS showed that surface chemistry of MPs dictates binding affinity. The key contributor to pepsin adsorption seems to be π−π interactions between the aromatic residues and the PS phenyl rings. During quick exposure (10 minutes) of pepsin to increasing concentrations (222, 2219, 22188 particles/mL) of 10 μm PS (PS10) and 100 μm PS (PS100), total enzymatic activities were not affected remarkably. However, upon prolonged exposure at 1 and 2 hours, preferential binding of pepsin to the small, low zeta-potential PS caused structural changes in the protein which led to a significant reduction of its activity. Digestion of cow’s milk mixed with PS10 resulted in transient accumulation of larger peptides (10-35 kDa) and reduced bioavailability of short peptides (2-9 kDa) in the gastric phase. This, however, was only observed at extremely high PS10 concentration (0.3 mg/mL or 5.46E+05 particles/mL). The digestion of milk peptides, bound preferentially over pepsin on the hard corona around PS10, was delayed up to 15 minutes in comparison to bulk protein digestion. Intact caseins, otherwise rapidly digested, remained bound to PS10 in hard corona for up to 15 minutes. This work presents valuable insights regarding the interaction of MPs, food proteins, and pepsin, and their dynamics during gastric digestion which provides new knowledge and understanding on the potential risks of MPs to human health.
HostingRepositoryPRIDE
AnnounceDate2024-03-19
AnnouncementXMLSubmission_2024-03-19_05:03:40.303.xml
DigitalObjectIdentifierhttps://dx.doi.org/10.6019/PXD041715
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportSupported dataset by repository
PrimarySubmitterTamara Vasovic
SpeciesList scientific name: Bos taurus (Bovine); NCBI TaxID: 9913;
ModificationListmonohydroxylated residue; deamidated residue; iodoacetamide derivatized residue
InstrumentOrbitrap Exploris 240
Dataset History
RevisionDatetimeStatusChangeLog Entry
02023-04-21 04:00:11ID requested
12024-03-19 05:03:40announced
Publication List
10.6019/PXD041715;
10.1016/J.ENVPOL.2023.122282;
Keyword List
submitter keyword: Microplastics
Milk proteins
LC-MS/MS
Simulated human gastric digestion
pepsin
polystyrene;
Contact List
Tanja Cirkovic Velickovic
contact affiliationProfessor of Biochemistry & Corresponding member of Serbian Academy of Sciences and Arts University of Belgrade-Faculty of Chemistry, Center of Excellence for Molecular Food Sciences and Department of Biochemistry, Studentski trg 12-16, 11 000 Belgrade, Serbia. Professor of Food Chemistry Department of Environmental Technology, Food Technology and Molecular Biotechnology, Ghent University Global Campus, Yeonsu-Gu, 21985 Incheon, Republic of Korea.
contact emailtcirkov@chem.bg.ac.rs
lab head
Tamara Vasovic
contact affiliationUniversity of Belgade - Faculty of Chemistry
contact emailtamara.vasovic@gmail.com
dataset submitter
Full Dataset Link List
Dataset FTP location
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