Dataset Information

Toxicity of true-to-life microplastics to human induced pluripotent stem cell -derived intestinal epithelia correlates to their protein corona composition

ABSTRACT: This study was conducted to determine the composition of the protein corona formed in cell culture medium on product-derived true-to-life microplastics and to link the functions of the protein corona to biological effects of true-to-life microplastics.

INSTRUMENT(S):

ORGANISM(S): Bos Taurus (bovine)

SUBMITTER: Sjef Boeren

LAB HEAD: Sjef Boeren

PROVIDER: PXD061584 | Pride | 2026-01-05

REPOSITORIES: Pride

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Publications

Toxicity of true-to-life microplastics to human iPSC-derived intestinal epithelia correlates to their protein corona composition.

Brouwer Hugo H Busch Mathias M Yang Shuo S Venus Tom T Aalderink Germaine G Crespo Juan Francisco Ferrer JFF Villacorta Aliro A Hernández Alba A Estrela-Lopis Irina I Boeren Sjef S Bouwmeester Hans H

Journal of hazardous materials 20250617

Humans are continually exposed to microplastics, now pervasive in the environment. The intestinal epithelium, as a primary barrier tissue, frequently faces high microplastic exposure, yet health implications remain elusive. Using an intestinal epithelial cell model derived from human induced pluripotent stem cells, we show intestinal toxicity upon exposure to true-to-life polyethylene terephthalate-TiO<sub>2</sub>, polypropylene-Talc, polyvinyl chloride and polyamide microplastics. These materia ...[more]

PMID: 40561950

Similar Datasets

Project description:The pollution of the environment with microplastics has been recognized as an emerging threat worldwide. Due to an exponential increase in production of plastic over the last eight decades and its longevity in the environment, accumulating amounts of microplastic are polluting rivers, lakes and the ocean. Their entry pathways are diverse and still only incompletely understood. Since microplastics are usually defined smaller than 5 mm, it can be ingested by a wide range of aquatic organisms including teleost fish. There are different approaches to study the detrimental effects of pollutants on aquatic organisms. On the one hand, generic baseline parameters such as growth and mortality are regularly considered, often accompanied by established stress parameters such as cortisol, heat shock proteins or lipid oxidation. The conflicting findings to date suggest that these parameters might not be sensitive enough to indicate the physiological effects of environmentally relevant microplastic concentrations. For this reason, more sophisticated biological approaches could provide new insights into whether and how microplastics harm fish. To date, proteomic approaches have been used only sporadically when investigating the effects of microplastic exposure on aquatic organisms. So far, this approach has not been used to address potential microplastic impacts in fish. In the present study, a proteomic approach was trialed alongside established methods in an investigation of fish experiencing long-term exposure to environmentally relevant concentrations of microplastics. Two groups of rainbow trout (Oncorhynchus mykiss were exposed to microplastic concentrations and sizes currently encountered in wild fish and an increased concentration, expected to occur in the near future. These groups where compared to a control group maintained in MP free conditions. Five fish of each treatment were sampled at three time points (week 1, week 4, week 17). The experiments were performed in triplicates, resulting in 45 samples used in the proteomic analysis.

Project description:Human 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.

			Action	DRS
	MQresult_Shuo28-51.zip	Other
	Shuo28_PVC1.raw	Raw
	Shuo29_PVC2.raw	Raw
	Shuo30_PVC3.raw	Raw
	Shuo31_PP1.raw	Raw